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Journal articles on the topic 'Syntrophin'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Peters, Matthew F., Marvin E. Adams, and Stanley C. Froehner. "Differential Association of Syntrophin Pairs with the Dystrophin Complex." Journal of Cell Biology 138, no. 1 (July 14, 1997): 81–93. http://dx.doi.org/10.1083/jcb.138.1.81.

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The syntrophins are a multigene family of intracellular dystrophin-associated proteins comprising three isoforms, α1, β1, and β2. Based on their domain organization and association with neuronal nitric oxide synthase, syntrophins are thought to function as modular adapters that recruit signaling proteins to the membrane via association with the dystrophin complex. Using sequences derived from a new mouse β1-syntrophin cDNA, and previously isolated cDNAs for α1- and β2-syntrophins, we prepared isoform-specific antibodies to study the expression, skeletal muscle localization, and dystrophin family association of all three syntrophins. Most tissues express multiple syntrophin isoforms. In mouse gastrocnemius skeletal muscle, α1- and β1-syntrophin are concentrated at the neuromuscular junction but are also present on the extrasynaptic sarcolemma. β1-syntrophin is restricted to fast-twitch muscle fibers, the first fibers to degenerate in Duchenne muscular dystrophy. β2-syntrophin is largely restricted to the neuromuscular junction. The sarcolemmal distribution of α1- and β1-syntrophins suggests association with dystrophin and dystrobrevin, whereas all three syntrophins could potentially associate with utrophin at the neuromuscular junction. Utrophin complexes immunoisolated from skeletal muscle are highly enriched in β1- and β2-syntrophins, while dystrophin complexes contain mostly α1- and β1-syntrophins. Dystrobrevin complexes contain dystrophin and α1- and β1-syntrophins. From these results, we propose a model in which a dystrophin–dystrobrevin complex is associated with two syntrophins. Since individual syntrophins do not have intrinsic binding specificity for dystrophin, dystrobrevin, or utrophin, the observed preferential pairing of syntrophins must depend on extrinsic regulatory mechanisms.

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2

Adams, Marvin E., Neal Kramarcy, Stuart P. Krall, Susana G. Rossi, Richard L. Rotundo, Robert Sealock, and Stanley C. Froehner. "Absence of α-Syntrophin Leads to Structurally Aberrant Neuromuscular Synapses Deficient in Utrophin." Journal of Cell Biology 150, no. 6 (September 18, 2000): 1385–98. http://dx.doi.org/10.1083/jcb.150.6.1385.

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The syntrophins are a family of structurally related proteins that contain multiple protein interaction motifs. Syntrophins associate directly with dystrophin, the product of the Duchenne muscular dystrophy locus, and its homologues. We have generated α-syntrophin null mice by targeted gene disruption to test the function of this association. The α-Syn−/− mice show no evidence of myopathy, despite reduced levels of α-dystrobrevin–2. Neuronal nitric oxide synthase, a component of the dystrophin protein complex, is absent from the sarcolemma of the α-Syn−/− mice, even where other syntrophin isoforms are present. α-Syn−/− neuromuscular junctions have undetectable levels of postsynaptic utrophin and reduced levels of acetylcholine receptor and acetylcholinesterase. The mutant junctions have shallow nerve gutters, abnormal distributions of acetylcholine receptors, and postjunctional folds that are generally less organized and have fewer openings to the synaptic cleft than controls. Thus, α-syntrophin has an important role in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse.

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3

Zhou, Yan Wen, Shilpa A. Oak, Susan E. Senogles, and Harry W. Jarrett. "Laminin-α1 globular domains 3 and 4 induce heterotrimeric G protein binding to α-syntrophin's PDZ domain and alter intracellular Ca2+ in muscle." American Journal of Physiology-Cell Physiology 288, no. 2 (February 2005): C377—C388. http://dx.doi.org/10.1152/ajpcell.00279.2004.

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α-Syntrophin is a component of the dystrophin glycoprotein complex (DGC). It is firmly attached to the dystrophin cytoskeleton via a unique COOH-terminal domain and is associated indirectly with α-dystroglycan, which binds to extracellular matrix laminin. Syntrophin contains two pleckstrin homology (PH) domains and one PDZ domain. Because PH domains of other proteins are known to bind the βγ-subunits of the heterotrimeric G proteins, whether this is also a property of syntrophin was investigated. Isolated syntrophin from rabbit skeletal muscle binds bovine brain Gβγ-subunits in gel blot overlay experiments. Laminin-1-Sepharose or specific antibodies against syntrophin, α- and β-dystroglycan, or dystrophin precipitate a complex with Gβγ from crude skeletal muscle microsomes. Bacterially expressed syntrophin fusion proteins and truncation mutants allowed mapping of Gβγ binding to syntrophin's PDZ domain; this is a novel function for PDZ domains. When laminin-1 is bound, maximal binding of Gsα and Gβγ occurs and active Gsα, measured as GTP-γ35S bound, decreases. Because intracellular Ca2+ is elevated in Duchenne muscular dystrophy and Gsα is known to activate the dihydropyridine receptor Ca2+ channel, whether laminin also altered intracellular Ca2+ was investigated. Laminin-1 decreases active (GTP-γS-bound) Gsα, and the Ca2+ channel is inhibited by laminin-1. The laminin α1-chain globular domains 4 and 5 region, the region bound by DGC α-dystroglycan, is sufficient to cause an effect, and an antibody that specifically blocks laminin binding to α-dystroglycan inhibits Gβ binding by syntrophin in C2C12 myotubes. These observations suggest that DGC is a matrix laminin, G protein-coupled receptor.

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4

Adams, Marvin E., Heather A. Mueller, and Stanley C. Froehner. "In vivo requirement of the α-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4." Journal of Cell Biology 155, no. 1 (September 24, 2001): 113–22. http://dx.doi.org/10.1083/jcb.200106158.

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α-Syntrophin is a scaffolding adapter protein expressed primarily on the sarcolemma of skeletal muscle. The COOH-terminal half of α-syntrophin binds to dystrophin and related proteins, leaving the PSD-95, discs-large, ZO-1 (PDZ) domain free to recruit other proteins to the dystrophin complex. We investigated the function of the PDZ domain of α-syntrophin in vivo by generating transgenic mouse lines expressing full-length α-syntrophin or a mutated α-syntrophin lacking the PDZ domain (ΔPDZ). The ΔPDZ α-syntrophin displaced endogenous α- and β1-syntrophin from the sarcolemma and resulted in sarcolemma containing little or no syntrophin PDZ domain. As a consequence, neuronal nitric oxide synthase (nNOS) and aquaporin-4 were absent from the sarcolemma. However, the sarcolemmal expression and distribution of muscle sodium channels, which bind the α-syntrophin PDZ domain in vitro, were not altered. Both transgenic mouse lines were bred with an α-syntrophin–null mouse which lacks sarcolemmal nNOS and aquaporin-4. The full-length α-syntrophin, not the ΔPDZ form, reestablished nNOS and aquaporin-4 at the sarcolemma of these mice. Genetic crosses with the mdx mouse showed that neither transgenic syntrophin could associate with the sarcolemma in the absence of dystrophin. Together, these data show that the sarcolemmal localization of nNOS and aquaporin-4 in vivo depends on the presence of a dystrophin-bound α-syntrophin PDZ domain.

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5

Peters, Matthew F., Neal R. Kramarcy, Robert Sealock, and Stanley C. Froehner. "β2-Syntrophin." NeuroReport 5, no. 13 (August 1994): 1577–80. http://dx.doi.org/10.1097/00001756-199408150-00009.

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6

Yakubchyk, Yury, Hanan Abramovici, Jean-Christian Maillet, Elias Daher, Christopher Obagi, Robin J. Parks, Matthew K. Topham, and Stephen H. Gee. "Regulation of Neurite Outgrowth in N1E-115 Cells through PDZ-Mediated Recruitment of Diacylglycerol Kinase ζ." Molecular and Cellular Biology 25, no. 16 (August 15, 2005): 7289–302. http://dx.doi.org/10.1128/mcb.25.16.7289-7302.2005.

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ABSTRACT Syntrophins are scaffold proteins that regulate the subcellular localization of diacylglycerol kinase ζ (DGK-ζ), an enzyme that phosphorylates the lipid second-messenger diacylglycerol to yield phosphatidic acid. DGK-ζ and syntrophins are abundantly expressed in neurons of the developing and adult brain, but their function is unclear. Here, we show that they are present in cell bodies, neurites, and growth cones of cultured cortical neurons and differentiated N1E-115 neuroblastoma cells. Overexpression of DGK-ζ in N1E-115 cells induced neurite formation in the presence of serum, which normally prevents neurite outgrowth. This effect was independent of DGK-ζ kinase activity but dependent on a functional C-terminal PDZ-binding motif, which specifically interacts with syntrophin PDZ domains. DGK-ζ mutants with a blocked C terminus acted as dominant-negative inhibitors of outgrowth from serum-deprived N1E-115 cells and cortical neurons. Several lines of evidence suggest DGK-ζ promotes neurite outgrowth through association with the GTPase Rac1. DGK-ζ colocalized with Rac1 in neuronal processes and DGK-ζ-induced outgrowth was inhibited by dominant-negative Rac1. Moreover, DGK-ζ directly interacts with Rac1 through a binding site located within its C1 domains. Together with syntrophin, these proteins form a tertiary complex in N1E-115 cells. A DGK-ζ mutant that mimics phosphorylation of the MARCKS domain was unable to bind an activated Rac1 mutant (Rac1V12) and phorbol myristate acetate-induced protein kinase C activation inhibited the interaction of DGK-ζ with Rac1V12, suggesting protein kinase C-mediated phosphorylation of the MARCKS domain negatively regulates DGK-ζ binding to active Rac1. Collectively, these findings suggest DGK-ζ, syntrophin, and Rac1 form a regulated signaling complex that controls polarized outgrowth in neuronal cells.

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7

Suzuki, A., M. Yoshida, and E. Ozawa. "Mammalian alpha 1- and beta 1-syntrophin bind to the alternative splice-prone region of the dystrophin COOH terminus." Journal of Cell Biology 128, no. 3 (February 1, 1995): 373–81. http://dx.doi.org/10.1083/jcb.128.3.373.

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The carboxy-terminal region of dystrophin has been suggested to be crucially important for its function to prevent muscle degeneration. We have previously shown that this region is the locus that interacts with the sarcolemmal glycoprotein complex, which mediates membrane anchoring of dystrophin, as well as with the cytoplasmic peripheral membrane protein, A0 and beta 1-syntrophin (Suzuki, A., M. Yoshida, K. Hayashi, Y. Mizuno, Y. Hagiwara, and E. Ozawa. 1994. Eur. J. Biochem. 220:283-292). In this work, by using the overlay assay technique developed previously, we further analyzed the dystrophin-syntrophin/A0 interaction. Two forms of mammalian syntrophin, alpha 1- and beta 1-syntrophin, were found to bind to very close but discrete regions on the dystrophin molecule. Their binding sites are located at the vicinity of the glycoprotein-binding site, and correspond to the amino acid residues encoded by exons 73-74 which are alternatively spliced out in some isoforms. This suggests that the function of syntrophin is tightly linked to the functional diversity among dystrophin isoforms. Pathologically, it is important that the binding site for alpha 1-syntrophin, which is predominantly expressed in skeletal muscle, coincides with the region whose deletion was suggested to result in a severe phenotype. In addition, A0, a minor component of dystrophin-associated proteins with a molecular mass of 94 kD which is immunochemically related to syntrophin, binds to the same site as beta 1-syntrophin. Finally, based on our accumulated evidence, we propose a revised model of the domain organization of dystrophin from the view point of protein-protein interactions.

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8

Kachinsky, Amy M., Stanley C. Froehner, and Sharon L. Milgram. "A PDZ-containing Scaffold Related to the Dystrophin Complex at the Basolateral Membrane of Epithelial Cells." Journal of Cell Biology 145, no. 2 (April 19, 1999): 391–402. http://dx.doi.org/10.1083/jcb.145.2.391.

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Membrane scaffolding complexes are key features of many cell types, serving as specialized links between the extracellular matrix and the actin cytoskeleton. An important scaffold in skeletal muscle is the dystrophin-associated protein complex. One of the proteins bound directly to dystrophin is syntrophin, a modular protein comprised entirely of interaction motifs, including PDZ (protein domain named for PSD-95, discs large, ZO-1) and pleckstrin homology (PH) domains. In skeletal muscle, the syntrophin PDZ domain recruits sodium channels and signaling molecules, such as neuronal nitric oxide synthase, to the dystrophin complex. In epithelia, we identified a variation of the dystrophin complex, in which syntrophin, and the dystrophin homologues, utrophin and dystrobrevin, are restricted to the basolateral membrane. We used exogenously expressed green fluorescent protein (GFP)-tagged fusion proteins to determine which domains of syntrophin are responsible for its polarized localization. GFP-tagged full-length syntrophin targeted to the basolateral membrane, but individual domains remained in the cytoplasm. In contrast, the second PH domain tandemly linked to a highly conserved, COOH-terminal region was sufficient for basolateral membrane targeting and association with utrophin. The results suggest an interaction between syntrophin and utrophin that leaves the PDZ domain of syntrophin available to recruit additional proteins to the epithelial basolateral membrane. The assembly of multiprotein signaling complexes at sites of membrane specialization may be a widespread function of dystrophin-related protein complexes.

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9

Ahn, A. H., and L. M. Kunkel. "Syntrophin binds to an alternatively spliced exon of dystrophin." Journal of Cell Biology 128, no. 3 (February 1, 1995): 363–71. http://dx.doi.org/10.1083/jcb.128.3.363.

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Dystrophin, the protein product of the Duchenne muscular dystrophy locus, is a protein of the membrane cytoskeleton that associates with a complex of integral and membrane-associated proteins. Of these, the 58-kD intracellular membrane-associated protein, syntrophin, was recently shown to consist of a family of three related but distinct genes. We expressed the cDNA of human beta 1-syntrophin and the COOH terminus of human dystrophin in reticulocyte lysates using an in vitro transcription/translation system. Using antibodies to dystrophin we immunoprecipitated these two interacting proteins in a variety of salt and detergent conditions. We demonstrate that the 53 amino acids encoded on exon 74 of dystrophin, an alternatively spliced exon, are necessary and sufficient for interaction with translated beta 1-syntrophin in our assay. On the basis of its alternative splicing, dystrophin may thus be present in two functionally distinct populations. In this recombinant expression system, the dystrophin relatives, human dystrophin related protein (DRP or utrophin) and the 87K postsynaptic protein from Torpedo electric organ, also bind to translated beta 1-syntrophin. We have found a COOH-terminal 37-kD fragment of beta 1-syntrophin sufficient to interact with translated dystrophin and its homologues, suggesting that the dystrophin binding site on beta 1-syntrophin occurs on a region that is conserved among the three syntrophin homologues.

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10

Luo, Shuo, Yu Chen, Kwok-On Lai, Juan Carlos Arévalo, Stanley C. Froehner, Marvin E. Adams, Moses V. Chao, and Nancy Y. Ip. "α-Syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner." Journal of Cell Biology 169, no. 5 (June 6, 2005): 813–24. http://dx.doi.org/10.1083/jcb.200412008.

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EphA4 signaling has recently been implicated in the regulation of synapse formation and plasticity. In this study, we show that ankyrin repeat-rich membrane spanning (ARMS; also known as a kinase D–interacting substrate of 220 kD), a substrate for ephrin and neurotrophin receptors, was expressed in developing muscle and was concentrated at the neuromuscular junction (NMJ). Using yeast two-hybrid screening, we identified a PDZ (PSD-95, Dlg, ZO-1) domain protein, α-syntrophin, as an ARMS-interacting protein in muscle. Overexpression of α-syntrophin induced ARMS clustering in a PDZ domain–dependent manner. Coexpression of ARMS enhanced EphA4 signaling, which was further augmented by the presence of α-syntrophin. Moreover, the ephrin-A1–induced tyrosine phosphorylation of EphA4 was reduced in C2C12 myotubes after the blockade of ARMS and α-syntrophin expression by RNA interference. Finally, α-syntrophin–null mice exhibited a disrupted localization of ARMS and EphA4 at the NMJ and a reduced expression of ARMS in muscle. Altogether, our findings suggest that ARMS may play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EphA4.

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11

Yang, Bin, Daniel Jung, Jill A. Rafael, Jeffrey S. Chamberlain, and Kevin P. Campbell. "Identification of α-Syntrophin Binding to Syntrophin Triplet, Dystrophin, and Utrophin." Journal of Biological Chemistry 270, no. 10 (March 10, 1995): 4975–78. http://dx.doi.org/10.1074/jbc.270.10.4975.

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12

Crawford, Gregory E., John A. Faulkner, Rachelle H. Crosbie, Kevin P. Campbell, Stanley C. Froehner, and Jeffrey S. Chamberlain. "Assembly of the Dystrophin-Associated Protein Complex Does Not Require the Dystrophin Cooh-Terminal Domain." Journal of Cell Biology 150, no. 6 (September 18, 2000): 1399–410. http://dx.doi.org/10.1083/jcb.150.6.1399.

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Dystrophin is a multidomain protein that links the actin cytoskeleton to laminin in the extracellular matrix through the dystrophin associated protein (DAP) complex. The COOH-terminal domain of dystrophin binds to two components of the DAP complex, syntrophin and dystrobrevin. To understand the role of syntrophin and dystrobrevin, we previously generated a series of transgenic mouse lines expressing dystrophins with deletions throughout the COOH-terminal domain. Each of these mice had normal muscle function and displayed normal localization of syntrophin and dystrobrevin. Since syntrophin and dystrobrevin bind to each other as well as to dystrophin, we have now generated a transgenic mouse deleted for the entire dystrophin COOH-terminal domain. Unexpectedly, this truncated dystrophin supported normal muscle function and assembly of the DAP complex. These results demonstrate that syntrophin and dystrobrevin functionally associate with the DAP complex in the absence of a direct link to dystrophin. We also observed that the DAP complexes in these different transgenic mouse strains were not identical. Instead, the DAP complexes contained varying ratios of syntrophin and dystrobrevin isoforms. These results suggest that alternative splicing of the dystrophin gene, which naturally generates COOH-terminal deletions in dystrophin, may function to regulate the isoform composition of the DAP complex.

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13

Newbell, Bobby J., J. Todd Anderson, and Harry W. Jarrett. "Ca2+-Calmodulin Binding to Mouse α1 Syntrophin: Syntrophin Is Also a Ca2+-Binding Protein†." Biochemistry 36, no. 6 (February 1997): 1295–305. http://dx.doi.org/10.1021/bi962452n.

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14

Hosaka, Yukio, Toshifumi Yokota, Yuko Miyagoe-Suzuki, Katsutoshi Yuasa, Michihiro Imamura, Ryoichi Matsuda, Takaaki Ikemoto, Shuhei Kameya, and Shin'ichi Takeda. "α1-Syntrophin–deficient skeletal muscle exhibits hypertrophy and aberrant formation of neuromuscular junctions during regeneration." Journal of Cell Biology 158, no. 6 (September 9, 2002): 1097–107. http://dx.doi.org/10.1083/jcb.200204076.

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α1-Syntrophin is a member of the family of dystrophin-associated proteins; it has been shown to recruit neuronal nitric oxide synthase and the water channel aquaporin-4 to the sarcolemma by its PSD-95/SAP-90, Discs-large, ZO-1 homologous domain. To examine the role of α1-syntrophin in muscle regeneration, we injected cardiotoxin into the tibialis anterior muscles of α1-syntrophin–null (α1syn−/−) mice. After the treatment, α1syn−/− muscles displayed remarkable hypertrophy and extensive fiber splitting compared with wild-type regenerating muscles, although the untreated muscles of the mutant mice showed no gross histological change. In the hypertrophied muscles of the mutant mice, the level of insulin-like growth factor-1 transcripts was highly elevated. Interestingly, in an early stage of the regeneration process, α1syn−/− mice showed remarkably deranged neuromuscular junctions (NMJs), accompanied by impaired ability to exercise. The contractile forces were reduced in α1syn−/− regenerating muscles. Our results suggest that the lack of α1-syntrophin might be responsible in part for the muscle hypertrophy, abnormal synapse formation at NMJs, and reduced force generation during regeneration of dystrophin-deficient muscle, all of which are typically observed in the early stages of Duchenne muscular dystrophy patients.

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15

Böhm, S. V., R. N. Sewduth, L. L. Zhuo, P. Constantinou, and R. G. Roberts. "P21 The relationship between syntrophins and syntrophin-binding sites (SBSs) in the dystrophins and dystrobrevins." Neuromuscular Disorders 20 (March 2010): S11. http://dx.doi.org/10.1016/s0960-8966(10)70036-5.

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16

Alessi, Amy, April D. Bragg, Justin M. Percival, Jean Yoo, Douglas E. Albrecht, Stanley C. Froehner, and Marvin E. Adams. "γ-Syntrophin scaffolding is spatially and functionally distinct from that of the α/β syntrophins." Experimental Cell Research 312, no. 16 (October 2006): 3084–95. http://dx.doi.org/10.1016/j.yexcr.2006.06.019.

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17

Costantini, Jennifer L., Samuel M. S. Cheung, Sen Hou, Hongzhao Li, Sam K. Kung, James B. Johnston, John A. Wilkins, Spencer B. Gibson, and Aaron J. Marshall. "TAPP2 links phosphoinositide 3-kinase signaling to B-cell adhesion through interaction with the cytoskeletal protein utrophin: expression of a novel cell adhesion-promoting complex in B-cell leukemia." Blood 114, no. 21 (November 19, 2009): 4703–12. http://dx.doi.org/10.1182/blood-2009-03-213058.

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Abstract Tandem pleckstrin homology domain proteins (TAPPs) are recruited to the plasma membrane via binding to phosphoinositides produced by phosphoinositide 3-kinases (PI3Ks). Whereas PI3Ks are critical for B-cell activation, the functions of TAPP proteins in B cells are unknown. We have identified 40 potential interaction partners of TAPP2 in B cells, including proteins involved in cytoskeletal rearrangement, signal transduction and endocytic trafficking. The association of TAPP2 with the cytoskeletal proteins utrophin and syntrophin was confirmed by Western blotting. We found that TAPP2, syntrophin, and utrophin are coexpressed in normal human B cells and B-chronic lymphocytic leukemia (B-CLL) cells. TAPP2 and syntrophin expression in B-CLL was variable from patient to patient, with significantly higher expression in the more aggressive disease subset identified by zeta-chain–associated protein kinase of 70 kDa (ZAP70) expression and unmutated immunoglobulin heavy chain (IgH) genes. We examined whether TAPP can regulate cell adhesion, a known function of utrophin/syntrophin in other cell types. Expression of membrane-targeted TAPP2 enhanced B-cell adhesion to fibronectin and laminin, whereas PH domain–mutant TAPP2 inhibited adhesion. siRNA knockdown of TAPP2 or utrophin, or treatment with PI3K inhibitors, significantly inhibited adhesion. These findings identify TAPP2 as a novel link between PI3K signaling and the cytoskeleton with potential relevance for leukemia progression.

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18

Chao, D. S., J. R. Gorospe, J. E. Brenman, J. A. Rafael, M. F. Peters, S. C. Froehner, E. P. Hoffman, J. S. Chamberlain, and D. S. Bredt. "Selective loss of sarcolemmal nitric oxide synthase in Becker muscular dystrophy." Journal of Experimental Medicine 184, no. 2 (August 1, 1996): 609–18. http://dx.doi.org/10.1084/jem.184.2.609.

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Becker muscular dystrophy is an X-linked disease due to mutations of the dystrophin gene. We now show that neuronal-type nitric oxide synthase (nNOS), an identified enzyme in the dystrophin complex, is uniquely absent from skeletal muscle plasma membrane in many human Becker patients and in mouse models of dystrophinopathy. An NH2-terminal domain of nNOS directly interacts with alpha 1-syntrophin but not with other proteins in the dystrophin complex analyzed. However, nNOS does not associate with alpha 1-syntrophin on the sarcolemma in transgenic mdx mice expressing truncated dystrophin proteins. This suggests a ternary interaction of nNOS, alpha 1-syntrophin, and the central domain of dystrophin in vivo, a conclusion supported by developmental studies in muscle. These data indicate that proper assembly of the dystrophin complex is dependent upon the structure of the central rodlike domain and have implications for the design of dystrophin-containing vectors for gene therapy.

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19

Munehira, Youichi, Tomohiro Ohnishi, Shinobu Kawamoto, Akiko Furuya, Kenya Shitara, Michihiro Imamura, Toshifumi Yokota, et al. "α1-Syntrophin Modulates Turnover of ABCA1." Journal of Biological Chemistry 279, no. 15 (January 13, 2004): 15091–95. http://dx.doi.org/10.1074/jbc.m313436200.

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20

Oak, Shilpa A., Katia Russo, Tamara C. Petrucci, and Harry W. Jarrett. "Mouse α1-Syntrophin Binding to Grb2: Further Evidence of a Role for Syntrophin in Cell Signaling†." Biochemistry 40, no. 37 (September 2001): 11270–78. http://dx.doi.org/10.1021/bi010490n.

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21

Blake, Derek J., Richard Hawkes, Matthew A. Benson, and Phillip W. Beesley. "Different Dystrophin-like Complexes Are Expressed in Neurons and Glia." Journal of Cell Biology 147, no. 3 (November 1, 1999): 645–58. http://dx.doi.org/10.1083/jcb.147.3.645.

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Duchenne muscular dystrophy is a fatal muscle disease that is often associated with cognitive impairment. Accordingly, dystrophin is found at the muscle sarcolemma and at postsynaptic sites in neurons. In muscle, dystrophin forms part of a membrane-spanning complex, the dystrophin-associated protein complex (DPC). Whereas the composition of the DPC in muscle is well documented, the existence of a similar complex in brain remains largely unknown. To determine the composition of DPC-like complexes in brain, we have examined the molecular associations and distribution of the dystrobrevins, a widely expressed family of dystrophin-associated proteins, some of which are components of the muscle DPC. β-Dystrobrevin is found in neurons and is highly enriched in postsynaptic densities (PSDs). Furthermore, β-dystrobrevin forms a specific complex with dystrophin and syntrophin. By contrast, α-dystrobrevin-1 is found in perivascular astrocytes and Bergmann glia, and is not PSD-enriched. α-Dystrobrevin-1 is associated with Dp71, utrophin, and syntrophin. In the brains of mice that lack dystrophin and Dp71, the dystrobrevin–syntrophin complexes are still formed, whereas in dystrophin-deficient muscle, the assembly of the DPC is disrupted. Thus, despite the similarity in primary sequence, α- and β-dystrobrevin are differentially distributed in the brain where they form separate DPC-like complexes.

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22

Claudepierre, T., C. Dalloz, D. Mornet, K. Matsumura, J. Sahel, and A. Rendon. "Characterization of the intermolecular associations of the dystrophin-associated glycoprotein complex in retinal Muller glial cells." Journal of Cell Science 113, no. 19 (October 1, 2000): 3409–17. http://dx.doi.org/10.1242/jcs.113.19.3409.

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The abnormal retinal neurotransmission observed in Duchenne muscular dystrophy patients has been attributed to altered expression of C-terminal products of the dystrophin gene in this tissue. Muller glial cells from rat retina express dystrophin protein Dp71, utrophin and the members of the dystrophin-associated glycoprotein complex (DGC), namely beta-dystroglycan, delta- and gamma-sarcoglycans and alpha1-syntrophin. The DGC could function in muscle as a link between the cystoskeleton and the extracellular matrix, as well as a signaling complex. However, other than in muscle the composition and intermolecular associations among members of the DGC are still unknown. Here we demonstrate that Dp71 and/or utrophin from rat retinal Muller glial cells form a complex with beta-dystroglycan, delta-sarcoglycan and alpha1-syntrophin. We also show that beta-dystroglycan is associated with alpha-dystrobrevin-1 and PSD-93 and that anti-PSD antibodies coimmunoprecipitated alpha-syntrophin with PSD-93. By overlay experiments we also found that Dp71and/or utrophin and alpha-dystroglycan from Muller cells could bind to actin and laminin, respectively. These results indicate that the DGC could have both structural and signaling functions in retina. On the basis of our accumulated evidence, we propose a hypothetical model for the molecular organization of the dystrophin-associated glycoprotein complex in retinal Muller glial cells, which would be helpful for understanding its function in the central nervous system.

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23

Kim, Min Jeong, Sung Ho Hwang, Jeong A. Lim, Stanley C. Froehner, Marvin E. Adams, and Hye Sun Kim. "α-Syntrophin Modulates Myogenin Expression in Differentiating Myoblasts." PLoS ONE 5, no. 12 (December 17, 2010): e15355. http://dx.doi.org/10.1371/journal.pone.0015355.

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Compton, Alison G., Sandra T. Cooper, Penelope M. Hill, Nan Yang, Stanley C. Froehner, and Kathryn N. North. "The Syntrophin-Dystrobrevin Subcomplex in Human Neuromuscular Disorders." Journal of Neuropathology & Experimental Neurology 64, no. 4 (April 2005): 350–61. http://dx.doi.org/10.1093/jnen/64.4.350.

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25

Hogan, Angela, Lynn Shepherd, Josée Chabot, Stéphane Quenneville, Stephen M. Prescott, Matthew K. Topham, and Stephen H. Gee. "Interaction of γ1-Syntrophin with Diacylglycerol Kinase-ζ." Journal of Biological Chemistry 276, no. 28 (May 14, 2001): 26526–33. http://dx.doi.org/10.1074/jbc.m104156200.

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26

Vandebrouck, Aurélie, Jessica Sabourin, Jéröme Rivet, Haouria Balghi, Stéphane Sebille, Alain Kitzis, Guy Raymond, Christian Cognard, Nicolas Bourmeyster, and Bruno Constantin. "Regulation of capacitative calcium entries by α1‐syntrophin: association of TRPC1 with dystrophin complex and the PDZ domain of α1‐syntrophin." FASEB Journal 21, no. 2 (January 3, 2007): 608–17. http://dx.doi.org/10.1096/fj.06-6683com.

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27

Zhou, Shan, and Lihsia Chen. "Neural integrity is maintained by dystrophin in C. elegans." Journal of Cell Biology 192, no. 2 (January 17, 2011): 349–63. http://dx.doi.org/10.1083/jcb.201006109.

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The dystrophin protein complex (DPC), composed of dystrophin and associated proteins, is essential for maintaining muscle membrane integrity. The link between mutations in dystrophin and the devastating muscle failure of Duchenne’s muscular dystrophy (DMD) has been well established. Less well appreciated are the accompanying cognitive impairment and neuropsychiatric disorders also presented in many DMD patients, which suggest a wider role for dystrophin in membrane–cytoskeleton function. This study provides genetic evidence of a novel role for DYS-1/dystrophin in maintaining neural organization in Caenorhabditis elegans. This neuronal function is distinct from the established role of DYS-1/dystrophin in maintaining muscle integrity and regulating locomotion. SAX-7, an L1 cell adhesion molecule (CAM) homologue, and STN-2/γ-syntrophin also function to maintain neural integrity in C. elegans. This study provides biochemical data that show that SAX-7 associates with DYS-1 in an STN-2/γ-syntrophin–dependent manner. These results reveal a recruitment of L1CAMs to the DPC to ensure neural integrity is maintained.

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28

Nagai, Rika, Reina Hashimoto, Yuko Tanaka, Osamu Taguchi, Mamiko Sato, Akio Matsukage, and Masamitsu Yamaguchi. "Syntrophin-2 is required for eye development in Drosophila." Experimental Cell Research 316, no. 2 (January 15, 2010): 272–85. http://dx.doi.org/10.1016/j.yexcr.2009.10.009.

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29

Adams, M. E. "Structural Abnormalities at Neuromuscular Synapses Lacking Multiple Syntrophin Isoforms." Journal of Neuroscience 24, no. 46 (November 17, 2004): 10302–9. http://dx.doi.org/10.1523/jneurosci.3408-04.2004.

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30

De Arcangelis, Valeria, Filippo Serra, Carlo Cogoni, Elisabetta Vivarelli, Lucia Monaco, and Fabio Naro. "β1-Syntrophin Modulation by miR-222 in mdx Mice." PLoS ONE 5, no. 8 (August 10, 2010): e12098. http://dx.doi.org/10.1371/journal.pone.0012098.

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31

Wu, Geru, Tomohiko Ai, Jeffrey J. Kim, Bhagyalaxmi Mohapatra, Yutao Xi, Zhaohui Li, Shahrzad Abbasi, et al. "α-1-Syntrophin Mutation and the Long-QT Syndrome." Circulation: Arrhythmia and Electrophysiology 1, no. 3 (August 2008): 193–201. http://dx.doi.org/10.1161/circep.108.769224.

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32

Torchio, Gabriela María, Mario Roberto Ermácora, and Mauricio Pablo Sica. "Equilibrium Unfolding of the PDZ Domain of β2-Syntrophin." Biophysical Journal 102, no. 12 (June 2012): 2835–44. http://dx.doi.org/10.1016/j.bpj.2012.05.021.

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33

Loh, Nellie Y., Daniela Nebenius-Oosthuizen, Derek J. Blake, Andrew J. H. Smith, and Kay E. Davies. "Role of β-Dystrobrevin in Nonmuscle Dystrophin-Associated Protein Complex-Like Complexes in Kidney and Liver." Molecular and Cellular Biology 21, no. 21 (November 1, 2001): 7442–48. http://dx.doi.org/10.1128/mcb.21.21.7442-7448.2001.

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ABSTRACT β-Dystrobrevin is a dystrophin-related and -associated protein that is highly expressed in brain, kidney, and liver. Recent studies with the kidneys of the mdx3Cv mouse, which lacks all dystrophin isoforms, suggest that β-dystrobrevin, and not the dystrophin isoforms, may be the key component in the assembly of complexes similar to the muscle dystrophin-associated protein complexes (DPC) in nonmuscle tissues. To understand the role of β-dystrobrevin in the function of nonmuscle tissues, we generated β-dystrobrevin-deficient (dtnb −/−) mice by gene targeting. dtnb −/− mice are healthy, fertile, and normal in appearance. No β-dystrobrevin was detected in these mice by Western blotting or immunocytochemistry. In addition, the levels of several β-dystrobrevin-interacting proteins, namely Dp71 isoforms and the syntrophins, were greatly reduced from the basal membranes of kidney tubules and liver sinusoids and on Western blots of crude kidney and liver microsomes of β-dystrobrevin-deficient mice. However, no abnormality was detected in the ultrastructure of membranes of kidney and liver cells or in the renal function of these mice. β-Dystrobrevin may therefore be an anchor or scaffold for Dp71 and syntrophin isoforms, as well as other associating proteins at the basal membranes of kidney and liver, but is not necessary for the normal function of these mice.

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34

Bhat, Hina F., Rafia A. Baba, Muneesa Bashir, Safder Saeed, Deeba Kirmani, Mudassir M. Wani, Nisar A. Wani, Khursheed A. Wani, and Firdous A. Khanday. "Alpha-1-syntrophin protein is differentially expressed in human cancers." Biomarkers 16, no. 1 (November 24, 2010): 31–36. http://dx.doi.org/10.3109/1354750x.2010.522731.

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35

Iwata, Yuko, Yan Pan, Tomokazu Yoshida, Hironori Hanada, and Munekazu Shigekawa. "α1-Syntrophin has distinct binding sites for actin and calmodulin." FEBS Letters 423, no. 2 (February 20, 1998): 173–77. http://dx.doi.org/10.1016/s0014-5793(98)00085-4.

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36

Eisinger, Kristina, Lisa Rein-Fischboeck, Rebekka Pohl, Elisabeth M. Meier, Sabrina Krautbauer, and Christa Buechler. "The adaptor protein alpha-syntrophin regulates adipocyte lipid droplet growth." Experimental Cell Research 345, no. 1 (July 2016): 100–107. http://dx.doi.org/10.1016/j.yexcr.2016.05.020.

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37

Hirn, Carole, George Shapovalov, Olivier Petermann, Emmanuelle Roulet, and Urs T. Ruegg. "Nav1.4 Deregulation in Dystrophic Skeletal Muscle Leads to Na+ Overload and Enhanced Cell Death." Journal of General Physiology 132, no. 2 (July 14, 2008): 199–208. http://dx.doi.org/10.1085/jgp.200810024.

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Duchenne muscular dystrophy (DMD) is a hereditary degenerative disease manifested by the absence of dystrophin, a structural, cytoskeletal protein, leading to muscle degeneration and early death through respiratory and cardiac muscle failure. Whereas the rise of cytosolic Ca2+ concentrations in muscles of mdx mouse, an animal model of DMD, has been extensively documented, little is known about the mechanisms causing alterations in Na+ concentrations. Here we show that the skeletal muscle isoform of the voltage-gated sodium channel, Nav1.4, which represents over 90% of voltage-gated sodium channels in muscle, plays an important role in development of abnormally high Na+ concentrations found in muscle from mdx mice. The absence of dystrophin modifies the expression level and gating properties of Nav1.4, leading to an increased Na+ concentration under the sarcolemma. Moreover, the distribution of Nav1.4 is altered in mdx muscle while maintaining the colocalization with one of the dystrophin-associated proteins, syntrophin α-1, thus suggesting that syntrophin is an important linker between dystrophin and Nav1.4. Additionally, we show that these modifications of Nav1.4 gating properties and increased Na+ concentrations are strongly correlated with increased cell death in mdx fibers and that both cell death and Na+ overload can be reversed by 3 nM tetrodotoxin, a specific Nav1.4 blocker.

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38

Gieseler, Kathrin, Manal Abdel-Dayem, and Laurent Ségalat. "In vitro interactions of Caenorhabditis elegans dystrophin with dystrobrevin and syntrophin." FEBS Letters 461, no. 1-2 (November 8, 1999): 59–62. http://dx.doi.org/10.1016/s0014-5793(99)01421-0.

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39

Ou, Yijun, Peter Strege, Steven M. Miller, Jonathan Makielski, Michael Ackerman, Simon J. Gibbons, and Gianrico Farrugia. "Syntrophin γ2 Regulates SCN5A Gating by a PDZ Domain-mediated Interaction." Journal of Biological Chemistry 278, no. 3 (November 11, 2002): 1915–23. http://dx.doi.org/10.1074/jbc.m209938200.

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40

Neely, J. D., M. Amiry-Moghaddam, O. P. Ottersen, S. C. Froehner, P. Agre, and M. E. Adams. "Syntrophin-dependent expression and localization of Aquaporin-4 water channel protein." Proceedings of the National Academy of Sciences 98, no. 24 (November 20, 2001): 14108–13. http://dx.doi.org/10.1073/pnas.241508198.

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41

Nakamori, M., T. Kimura, T. Kubota, T. Matsumura, H. Sumi, H. Fujimura, M. P. Takahashi, and S. Sakoda. "Aberrantly spliced -dystrobrevin alters -syntrophin binding in myotonic dystrophy type 1." Neurology 70, no. 9 (February 25, 2008): 677–85. http://dx.doi.org/10.1212/01.wnl.0000302174.08951.cf.

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42

Gee, Stephen H., Stacy A. Sekely, Christian Lombardo, Alexei Kurakin, Stanley C. Froehner, and Brian K. Kay. "Cyclic Peptides as Non-carboxyl-terminal Ligands of Syntrophin PDZ Domains." Journal of Biological Chemistry 273, no. 34 (August 21, 1998): 21980–87. http://dx.doi.org/10.1074/jbc.273.34.21980.

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43

Bhat, Hina F., Marvin E. Adams, and Firdous A. Khanday. "Syntrophin proteins as Santa Claus: role(s) in cell signal transduction." Cellular and Molecular Life Sciences 70, no. 14 (December 21, 2012): 2533–54. http://dx.doi.org/10.1007/s00018-012-1233-9.

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44

Rein-Fischboeck, Lisa, Ganimete Bajraktari, Rebekka Pohl, Susanne Feder, Kristina Eisinger, Wolfgang Mages, Elisabeth M. Haberl, and Christa Buechler. "Alpha-syntrophin dependent expression of tubulin alpha 8 protein in hepatocytes." Journal of Physiology and Biochemistry 74, no. 4 (July 22, 2018): 511–21. http://dx.doi.org/10.1007/s13105-018-0645-x.

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45

Hori, Tomoyuki, Daisuke Sasaki, Shin Haruta, Toru Shigematsu, Yoshiyuki Ueno, Masaharu Ishii, and Yasuo Igarashi. "Detection of active, potentially acetate-oxidizing syntrophs in an anaerobic digester by flux measurement and formyltetrahydrofolate synthetase (FTHFS) expression profiling." Microbiology 157, no. 7 (July 1, 2011): 1980–89. http://dx.doi.org/10.1099/mic.0.049189-0.

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Syntrophic oxidation of acetate, so-called reversed reductive acetogenesis, is one of the most important degradation steps in anaerobic digesters. However, little is known about the genetic diversity of the micro-organisms involved. Here we investigated the activity and composition of potentially acetate-oxidizing syntrophs using a combinatorial approach of flux measurement and transcriptional profiling of the formyltetrahydrofolate synthetase (FTHFS) gene, an ecological biomarker for reductive acetogenesis. During the operation of a thermophilic anaerobic digester, volatile fatty acids were mostly depleted, suggesting a high turnover rate for dissolved H2, and hydrogenotrophic methanogens were the dominant archaeal members. Batch cultivation of the digester microbiota with 13C-labelled acetate indicated that syntrophic oxidation accounted for 13.1–21.3 % of methane production from acetate. FTHFS genes were transcribed in the absence of carbon monoxide, methoxylated compounds and inorganic electron acceptors other than CO2, which is implicated in the activity of reversed reductive acetogenesis; however, expression itself does not distinguish whether biosynthesis or biodegradation is functioning. The mRNA- and DNA-based terminal RFLP and clone library analyses indicated that, out of nine FTHFS phylotypes detected, the FTHFS genes from the novel phylotypes I–IV in addition to the known syntroph Thermacetogenium phaeum (i.e. phylotype V) were specifically expressed. These transcripts arose from phylogenetically presumed homoacetogens. The results of this study demonstrate that hitherto unidentified phylotypes of homoacetogens are responsible for syntrophic acetate oxidation in an anaerobic digester.

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46

Ishii, Shun'ichi, Tomoyuki Kosaka, Yasuaki Hotta, and Kazuya Watanabe. "Simulating the Contribution of Coaggregation to Interspecies Hydrogen Fluxes in Syntrophic Methanogenic Consortia." Applied and Environmental Microbiology 72, no. 7 (July 2006): 5093–96. http://dx.doi.org/10.1128/aem.00333-06.

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ABSTRACT A simple model (termed the syntrophy model) for simulating the contribution of coaggregation to interspecies hydrogen fluxes between syntrophic bacteria and methanogenic archaea is described. We applied it to analyzing partially aggregated syntrophic cocultures with various substrates, revealing that large fractions of hydrogen molecules were fluxed in aggregates.

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47

Hao, Liping, Thomas Yssing Michaelsen, Caitlin Margaret Singleton, Giulia Dottorini, Rasmus Hansen Kirkegaard, Mads Albertsen, Per Halkjær Nielsen, and Morten Simonsen Dueholm. "Novel syntrophic bacteria in full-scale anaerobic digesters revealed by genome-centric metatranscriptomics." ISME Journal 14, no. 4 (January 2, 2020): 906–18. http://dx.doi.org/10.1038/s41396-019-0571-0.

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AbstractShort-chain fatty acid (SCFA) degradation is an important process in methanogenic ecosystems, and is usually catalyzed by SCFA-oxidizing bacteria in syntrophy with methanogens. Current knowledge of this functional guild is mainly based on isolates or enrichment cultures, but these may not reflect the true diversity and in situ activities of the syntrophs predominating in full-scale systems. Here we obtained 182 medium to high quality metagenome-assembled genomes (MAGs) from the microbiome of two full-scale anaerobic digesters. The transcriptomic response of individual MAG was studied after stimulation with low concentrations of acetate, propionate, or butyrate, separately. The most pronounced response to butyrate was observed for two MAGs of the recently described genus Candidatus Phosphitivorax (phylum Desulfobacterota), expressing a butyrate beta-oxidation pathway. For propionate, the largest response was observed for an MAG of a novel genus in the family Pelotomaculaceae, transcribing a methylmalonyl-CoA pathway. All three species were common in anaerobic digesters at Danish wastewater treatment plants as shown by amplicon analysis, and this is the first time their syntrophic features involved in SCFA oxidation were revealed with transcriptomic evidence. Further, they also possessed unique genomic features undescribed in well-characterized syntrophs, including the metabolic pathways for phosphite oxidation, nitrite and sulfate reduction.

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48

Chockalingam, Priya Sethu, Stephen H. Gee, and Harry W. Jarrett. "Pleckstrin Homology Domain 1 of Mouse α1-Syntrophin Binds Phosphatidylinositol 4,5-Bisphosphate†." Biochemistry 38, no. 17 (April 1999): 5596–602. http://dx.doi.org/10.1021/bi982564+.

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49

Hashida-Okumura, Akiko, Nobuaki Okumura, Akihiro Iwamatsu, Ruud M. Buijs, Herms J. Romijn, and Katsuya Nagai. "Interaction of Neuronal Nitric-oxide Synthase with α1-Syntrophin in Rat Brain." Journal of Biological Chemistry 274, no. 17 (April 23, 1999): 11736–41. http://dx.doi.org/10.1074/jbc.274.17.11736.

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50

Martinez-Pena y Valenzuela, I., C. Mouslim, M. Pires-Oliveira, M. E. Adams, S. C. Froehner, and M. Akaaboune. "Nicotinic Acetylcholine Receptor Stability at the NMJ Deficient in -Syntrophin In Vivo." Journal of Neuroscience 31, no. 43 (October 26, 2011): 15586–96. http://dx.doi.org/10.1523/jneurosci.4038-11.2011.

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