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Relevant bibliographies by topics / SAnk1.5

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Academic literature on the topic 'SAnk1.5'

Author: Grafiati

Published: 14 March 2023

Last updated: 31 July 2025

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Journal articles on the topic "SAnk1.5"

1

Lange, Stephan, Sue Perera, Phildrich Teh, and Ju Chen. "Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover." Molecular Biology of the Cell 23, no. 13 (2012): 2490–504. http://dx.doi.org/10.1091/mbc.e12-01-0052.

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Protein turnover through cullin-3 is tightly regulated by posttranslational modifications, the COP9 signalosome, and BTB/POZ-domain proteins that link cullin-3 to specific substrates for ubiquitylation. In this paper, we report how potassium channel tetramerization domain containing 6 (KCTD6) represents a novel substrate adaptor for cullin-3, effectively regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5).Binding of sAnk1.5 to KCTD6, and its subsequent turnover is regulated through posttranslational modification by nedd8, ubiquitin, and acetylation of C-terminal lysine

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2

Gokhin, David S., та Velia M. Fowler. "Cytoplasmic γ-actin and tropomodulin isoforms link to the sarcoplasmic reticulum in skeletal muscle fibers". Journal of Cell Biology 194, № 1 (2011): 105–20. http://dx.doi.org/10.1083/jcb.201011128.

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The sarcoplasmic reticulum (SR) serves as the Ca2+ reservoir for muscle contraction. Tropomodulins (Tmods) cap filamentous actin (F-actin) pointed ends, bind tropomyosins (Tms), and regulate F-actin organization. In this paper, we use a genetic targeting approach to examine the effect of Tmod1 deletion on the organization of cytoplasmic γ-actin (γcyto-actin) in the SR of skeletal muscle. In wild-type muscle fibers, γcyto-actin and Tmod3 defined an SR microdomain that was distinct from another Z line–flanking SR microdomain containing Tmod1 and Tmod4. The γcyto-actin/Tmod3 microdomain contained

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3

Giacomello, E., M. Quarta, C. Paolini, et al. "Deletion of small ankyrin 1 (sAnk1) isoforms results in structural and functional alterations in aging skeletal muscle fibers." American Journal of Physiology-Cell Physiology 308, no. 2 (2015): C123—C138. http://dx.doi.org/10.1152/ajpcell.00090.2014.

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Muscle-specific ankyrins 1 (sAnk1) are a group of small ankyrin 1 isoforms, of which sAnk1.5 is the most abundant. sAnk1 are localized in the sarcoplasmic reticulum (SR) membrane from where they interact with obscurin, a myofibrillar protein. This interaction appears to contribute to stabilize the SR close to the myofibrils. Here we report the structural and functional characterization of skeletal muscles from sAnk1 knockout mice (KO). Deletion of sAnk1 did not change the expression and localization of SR proteins in 4- to 6-mo-old sAnk1 KO mice. Structurally, the main modification observed in

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4

Randazzo, Davide, Emiliana Giacomello, Stefania Lorenzini, et al. "Obscurin is required for ankyrinB-dependent dystrophin localization and sarcolemma integrity." Journal of Cell Biology 200, no. 4 (2013): 523–36. http://dx.doi.org/10.1083/jcb.201205118.

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Obscurin is a large myofibrillar protein that contains several interacting modules, one of which mediates binding to muscle-specific ankyrins. Interaction between obscurin and the muscle-specific ankyrin sAnk1.5 regulates the organization of the sarcoplasmic reticulum in striated muscles. Additional muscle-specific ankyrin isoforms, ankB and ankG, are localized at the subsarcolemma level, at which they contribute to the organization of dystrophin and β-dystroglycan at costameres. In this paper, we report that in mice deficient for obscurin, ankB was displaced from its localization at the M ban

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5

Pierantozzi, Enrico, Péter Szentesi, Dána Al-Gaadi, et al. "Calcium Homeostasis Is Modified in Skeletal Muscle Fibers of Small Ankyrin1 Knockout Mice." International Journal of Molecular Sciences 20, no. 13 (2019): 3361. http://dx.doi.org/10.3390/ijms20133361.

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Small Ankyrins (sAnk1) are muscle-specific isoforms generated by the Ank1 gene that participate in the organization of the sarcoplasmic reticulum (SR) of striated muscles. Accordingly, the volume of SR tubules localized around the myofibrils is strongly reduced in skeletal muscle fibers of 4- and 10-month-old sAnk1 knockout (KO) mice, while additional structural alterations only develop with aging. To verify whether the lack of sAnk1 also alters intracellular Ca2+ handling, cytosolic Ca2+ levels were analyzed in stimulated skeletal muscle fibers from 4- and 10-month-old sAnk1 KO mice. The SR C

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6

Kontrogianni-Konstantopoulos, Aikaterini, Ellene M. Jones, Damian B. van Rossum, and Robert J. Bloch. "Obscurin Is a Ligand for Small Ankyrin 1 in Skeletal Muscle." Molecular Biology of the Cell 14, no. 3 (2003): 1138–48. http://dx.doi.org/10.1091/mbc.e02-07-0411.

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The factors that organize the internal membranes of cells are still poorly understood. We have been addressing this question using striated muscle cells, which have regular arrays of membranes that associate with the contractile apparatus in stereotypic patterns. Here we examine links between contractile structures and the sarcoplasmic reticulum (SR) established by small ankyrin 1 (sAnk1), a ∼17.5-kDa integral protein of network SR. We used yeast two-hybrid to identify obscurin, a giant Rho-GEF protein, as the major cytoplasmic ligand for sAnk1. The binding of obscurin to the cytoplasmic seque

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7

Pierantozzi, E., L. Raucci, S. Buonocore, et al. "Skeletal muscle overexpression of sAnk1.5 in transgenic mice does not predispose to type 2 diabetes." Scientific Reports 13, no. 1 (2023). http://dx.doi.org/10.1038/s41598-023-35393-0.

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AbstractGenome-wide association studies (GWAS) and cis-expression quantitative trait locus (cis-eQTL) analyses indicated an association of the rs508419 single nucleotide polymorphism (SNP) with type 2 diabetes (T2D). rs508419 is localized in the muscle-specific internal promoter (P2) of the ANK1 gene, which drives the expression of the sAnk1.5 isoform. Functional studies showed that the rs508419 C/C variant results in increased transcriptional activity of the P2 promoter, leading to higher levels of sAnk1.5 mRNA and protein in skeletal muscle biopsies of individuals carrying the C/C genotype.

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8

Li, Yi, Amanda Labuza, Nathan Wright, and Robert Bloch. "Regulation of SERCA1 in Skeletal Muscle by sAnk1: Binding to Phospholamban and the Role of sAnk1’s Cytoplasmic Domain." Physiology 40, S1 (2025). https://doi.org/10.1152/physiol.2025.40.s1.2073.

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Sarcoplasmic/endoplasmic reticulum Ca 2+ -ATPase1 (SERCA1) is responsible for the clearance of cytosolic Ca 2+ in skeletal muscle, and its regulation has been intensively studied. Small ankyrin 1 (sAnk1, Ank1.5), a 17 kDa muscle-specific isoform of ANK1, binds to SERCA1 directly via both its transmembrane and cytoplasmic domains and inhibits SERCA1’s ATPase activity. We characterized the interaction between the cytoplasmic domain of sAnk1 (sAnk1(29-155)) and SERCA1. The binding affinity was 444 nM by blot overlay, about 7-fold weaker than the binding of sAnk1(29-155) to obscurin, a giant prote

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9

Toral-Ojeda, Ivan, Garazi Aldanondo, Jaione Lasa-Elgarresta, et al. "Calpain 3 deficiency affects SERCA expression and function in the skeletal muscle." Expert Reviews in Molecular Medicine 18 (2016). http://dx.doi.org/10.1017/erm.2016.9.

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Limb-girdle muscular dystrophy type 2A (LGMD2A) is a form of muscular dystrophy caused by mutations in calpain 3 (CAPN3). Several studies have implicated Ca2+ dysregulation as an underlying event in several muscular dystrophies, including LGMD2A. In this study we used mouse and human myotube cultures, and muscle biopsies in order to determine whether dysfunction of sarco/endoplasmatic Ca2+-ATPase (SERCA) is involved in the pathology of this disease. In CAPN3-deficient myotubes, we found decreased levels of SERCA 1 and 2 proteins, while mRNA levels remained comparable with control myotubes. Als

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Guo, Xiaoping, Ganqiu Lan, Qinyang Jiang, et al. "Expression mechanisms of mir-486-5p and its host gene sANK1 in porcine muscle." Molecular Biology Reports 51, no. 1 (2024). http://dx.doi.org/10.1007/s11033-024-09773-2.

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Dissertations / Theses on the topic "SAnk1.5"

1

buonocore, sara. "The ANK1 rs508419-C T2D-risk allele increases the expression of sAnk1.5 and miR486 but their overexpression in transgenic mice does not significantly alter glucose tolerance." Doctoral thesis, Università di Siena, 2022. http://hdl.handle.net/11365/1211536.

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Genome wide association studies (GWAS) identified the ANK1 gene as a common type 2 diabetes mellitus (T2D) susceptibility locus. More recently, GWAS studies identified a novel SNP associated to T2D susceptibility, namely rs508419, in the internal promoter of ANK1 gene, which drives the expression of small ankyrin 1.5 (sAnk1.5), a striated muscle-specific protein localized in the sarcoplasmic reticulum (SR) membrane. sAnk1.5 interacts with the giant sarcomeric protein obscurin, allowing the correct localization of SR around the myofibrils. The rs508419 SNP is characterized by the substitu

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2

Raucci, Luisa. "Increased expression of sAnk1.5 does not predispose to Type 2 Diabetes in transgenic mice." Doctoral thesis, Università di Siena, 2020. http://hdl.handle.net/11365/1106623.

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Skeletal muscle represents about 40% of the body mass and is the site where the major part of blood glucose is disposed following insulin stimulation. Due to this critical role, skeletal muscle dysfunctions often result in the development of systemic metabolic diseases. Type 2 Diabetes (T2D) is the most common chronic metabolic disorder, representing nearly 90% of the overall diabetes cases. T2D is characterized by insulin resistance followed by reduced insulin release from pancreatic b-cells, resulting in high glucose concentration in bloodstream and glucose intolerance. T2D is a multi

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