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Journal articles on the topic 'Spectrin'

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Published: 4 June 2021

Last updated: 25 May 2024

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1

Machnicka, Beata, Renata Grochowalska, Dżamila M. Bogusławska, and Aleksander F. Sikorski. "The role of spectrin in cell adhesion and cell–cell contact." Experimental Biology and Medicine 244, no. 15 (June 21, 2019): 1303–12. http://dx.doi.org/10.1177/1535370219859003.

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Spectrins are proteins that are responsible for many aspects of cell function and adaptation to changing environments. Primarily the spectrin-based membrane skeleton maintains cell membrane integrity and its mechanical properties, together with the cytoskeletal network a support cell shape. The occurrence of a variety of spectrin isoforms in diverse cellular environments indicates that it is a multifunctional protein involved in numerous physiological pathways. Participation of spectrin in cell–cell and cell–extracellular matrix adhesion and formation of dynamic plasma membrane protrusions and

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2

Goodman, Steven R., Daniel Johnson, Steven L. Youngentob, and David Kakhniashvili. "The Spectrinome: The Interactome of a Scaffold Protein Creating Nuclear and Cytoplasmic Connectivity and Function." Experimental Biology and Medicine 244, no. 15 (September 4, 2019): 1273–302. http://dx.doi.org/10.1177/1535370219867269.

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We provide a review of Spectrin isoform function in the cytoplasm, the nucleus, the cell surface, and in intracellular signaling. We then discuss the importance of Spectrin’s E2/E3 chimeric ubiquitin conjugating and ligating activity in maintaining cellular homeostasis. Finally we present spectrin isoform subunit specific human diseases. We have created the Spectrinome, from the Human Proteome, Human Reactome and Human Atlas data and demonstrated how it can be a useful tool in visualizing and understanding spectrins myriad of cellular functions. Impact statement Spectrin was for the first 12 y

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3

Moorthy, Suraj, Lihsia Chen та Vann Bennett. "Caenorhabditis elegans β-G Spectrin Is Dispensable for Establishment of Epithelial Polarity, but Essential for Muscular and Neuronal Function". Journal of Cell Biology 149, № 4 (15 травня 2000): 915–30. http://dx.doi.org/10.1083/jcb.149.4.915.

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The Caenorhabditis elegans genome encodes one α spectrin subunit, a β spectrin subunit (β-G), and a β-H spectrin subunit. Our experiments show that the phenotype resulting from the loss of the C. elegans α spectrin is reproduced by tandem depletion of both β-G and β-H spectrins. We propose that α spectrin combines with the β-G and β-H subunits to form α/β-G and α/β-H heteromers that perform the entire repertoire of spectrin function in the nematode. The expression patterns of nematode β-G spectrin and vertebrate β spectrins exhibit three striking parallels including: (1) β spectrins are associ

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Nicolas, Gaël, Catherine M. Fournier, Colette Galand, Laurence Malbert-Colas, Odile Bournier, Yolande Kroviarski, Monique Bourgeois, et al. "Tyrosine Phosphorylation Regulates Alpha II Spectrin Cleavage by Calpain." Molecular and Cellular Biology 22, no. 10 (May 15, 2002): 3527–36. http://dx.doi.org/10.1128/mcb.22.10.3527-3536.2002.

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ABSTRACT Spectrins, components of the membrane skeleton, are implicated in various cellular functions. Understanding the diversity of these functions requires better characterization of the interacting domains of spectrins, such as the SH3 domain. Yeast two-hybrid screening of a kidney cDNA library revealed that the SH3 domain of αII-spectrin binds specifically isoform A of low-molecular-weight phosphotyrosine phosphatase (LMW-PTP). The αII-spectrin SH3 domain does not interact with LMW-PTP B or C nor does LMW-PTP A interact with the αI-spectrin SH3 domain. The interaction of spectrin with LMW

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5

Leto, T. L., D. Fortugno-Erikson, D. Barton, T. L. Yang-Feng, U. Francke, A. S. Harris, J. S. Morrow, V. T. Marchesi, and E. J. Benz. "Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species." Molecular and Cellular Biology 8, no. 1 (January 1988): 1–9. http://dx.doi.org/10.1128/mcb.8.1.1-9.1988.

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The spectrins are a family of widely distributed filamentous proteins. In association with actin, spectrins form a supporting and organizing scaffold for cell membranes. Using antibodies specific for human brain alpha-spectrin (alpha-fodrin), we have cloned a rat brain alpha-spectrin cDNA from an expression library. Several closely related human clones were also isolated by hybridization. Comparison of sequences of these and other overlapping nonerythroid and erythroid alpha-spectrin genes demonstrated that the nonerythroid genes are strictly conserved across species, while the mammalian eryth

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6

Leto, T. L., D. Fortugno-Erikson, D. Barton, T. L. Yang-Feng, U. Francke, A. S. Harris, J. S. Morrow, V. T. Marchesi, and E. J. Benz. "Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species." Molecular and Cellular Biology 8, no. 1 (January 1988): 1–9. http://dx.doi.org/10.1128/mcb.8.1.1.

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The spectrins are a family of widely distributed filamentous proteins. In association with actin, spectrins form a supporting and organizing scaffold for cell membranes. Using antibodies specific for human brain alpha-spectrin (alpha-fodrin), we have cloned a rat brain alpha-spectrin cDNA from an expression library. Several closely related human clones were also isolated by hybridization. Comparison of sequences of these and other overlapping nonerythroid and erythroid alpha-spectrin genes demonstrated that the nonerythroid genes are strictly conserved across species, while the mammalian eryth

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7

Kennedy, S. P., S. L. Warren, B. G. Forget, and J. S. Morrow. "Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin." Journal of Cell Biology 115, no. 1 (October 1, 1991): 267–77. http://dx.doi.org/10.1083/jcb.115.1.267.

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Ankyrin mediates the attachment of spectrin to transmembrane integral proteins in both erythroid and nonerythroid cells by binding to the beta-subunit of spectrin. Previous studies using enzymatic digestion, 2-nitro-5-thiocyanobenzoic acid cleavage, and rotary shadowing techniques have placed the spectrin-ankyrin binding site in the COOH-terminal third of beta-spectrin, but the precise site is not known. We have used a glutathione S-transferase prokaryotic expression system to prepare recombinant erythroid and nonerythroid beta-spectrin from cDNA encoding approximately the carboxy-terminal hal

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8

Howe, C. L., L. M. Sacramone, M. S. Mooseker, and J. S. Morrow. "Mechanisms of cytoskeletal regulation: modulation of membrane affinity in avian brush border and erythrocyte spectrins." Journal of Cell Biology 101, no. 4 (October 1, 1985): 1379–85. http://dx.doi.org/10.1083/jcb.101.4.1379.

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The spectrins isolated from chicken erythrocytes and chicken intestinal brush border, TW260/240, share a common alpha subunit and a tissue-specific beta subunit. The ability of these related proteins to bind human erythrocyte inside out vesicles (IOVs) and human erythrocyte ankyrin in vitro have been quantitatively compared with human erythrocyte spectrin. Chicken erythrocyte spectrin binds human IOVs and human ankyrin with affinities nearly identical to that for human erythrocyte spectrin. TW260/240 does not significantly bind to either IOVs or ankyrin. These results demonstrate a remarkable

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9

Baines, Anthony J. "Evolution of spectrin function in cytoskeletal and membrane networks." Biochemical Society Transactions 37, no. 4 (July 22, 2009): 796–803. http://dx.doi.org/10.1042/bst0370796.

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Spectrin is a cytoskeletal protein thought to have descended from an α-actinin-like ancestor. It emerged during evolution of animals to promote integration of cells into tissues by assembling signalling and cell adhesion complexes, by enhancing the mechanical stability of membranes and by promoting assembly of specialized membrane domains. Spectrin functions as an (αβ[H])2 tetramer that cross-links transmembrane proteins, membrane lipids and the actin cytoskeleton, either directly or via adaptor proteins such as ankyrin and 4.1. In the present paper, I review recent findings on the origins and

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Lawler, J., TL Coetzer, VN Mankad, RB Moore, JT Prchal, and J. Palek. "Spectrin-alpha I/61: a new structural variant of alpha-spectrin in a double-heterozygous form of hereditary pyropoikilocytosis." Blood 72, no. 4 (October 1, 1988): 1412–15. http://dx.doi.org/10.1182/blood.v72.4.1412.1412.

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Abstract Recent biochemical studies have led to the identification of abnormal spectrins in the erythrocytes of patients with hereditary pyropoikilocytosis (HPP) and hereditary elliptocytosis (HE). In this report we describe the biochemical characterization of the erythrocytes from a proband with severe HPP who is doubly heterozygous for two mutant spectrins (Sp): Sp alpha I/74 and a new, previously undetected, mutant of alpha-spectrin designated Sp alpha I/61. The proband's erythrocytes are unstable when exposed to 45 degrees C, and her membrane skeletons exhibit instability to shear stress.

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Lawler, J., TL Coetzer, VN Mankad, RB Moore, JT Prchal, and J. Palek. "Spectrin-alpha I/61: a new structural variant of alpha-spectrin in a double-heterozygous form of hereditary pyropoikilocytosis." Blood 72, no. 4 (October 1, 1988): 1412–15. http://dx.doi.org/10.1182/blood.v72.4.1412.bloodjournal7241412.

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Recent biochemical studies have led to the identification of abnormal spectrins in the erythrocytes of patients with hereditary pyropoikilocytosis (HPP) and hereditary elliptocytosis (HE). In this report we describe the biochemical characterization of the erythrocytes from a proband with severe HPP who is doubly heterozygous for two mutant spectrins (Sp): Sp alpha I/74 and a new, previously undetected, mutant of alpha-spectrin designated Sp alpha I/61. The proband's erythrocytes are unstable when exposed to 45 degrees C, and her membrane skeletons exhibit instability to shear stress. The conte

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Coleman, T. R., A. S. Harris, S. M. Mische, M. S. Mooseker, and J. S. Morrow. "Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions." Journal of Cell Biology 104, no. 3 (March 1, 1987): 519–26. http://dx.doi.org/10.1083/jcb.104.3.519.

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The ability of protein 4.1 to stimulate the binding of spectrin to F-actin has been compared by cosedimentation analysis for three avian (erythrocyte, brain, and brush border) and two mammalian (erythrocyte and brain) spectrin isoforms. Human erythroid protein 4.1 stimulated actin binding of all spectrins except the brush border isoform (TW 260/240). These results suggested that the beta subunit determined the protein 4.1 sensitivity of the heterodimer, since all avian alpha subunits are encoded by a single gene. Tissue-specific posttranslational modification of the alpha subunit was excluded

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13

Zhou, Daixing, Jeanine A. Ursitti, and Robert J. Bloch. "Developmental Expression of Spectrins in Rat Skeletal Muscle." Molecular Biology of the Cell 9, no. 1 (January 1998): 47–61. http://dx.doi.org/10.1091/mbc.9.1.47.

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Skeletal muscle contains spectrin (or spectrin I) and fodrin (or spectrin II), members of the spectrin supergene family. We used isoform-specific antibodies and cDNA probes to investigate the molecular forms, developmental expression, and subcellular localization of the spectrins in skeletal muscle of the rat. We report that β-spectrin (βI) replaces β-fodrin (βII) at the sarcolemma as skeletal muscle fibers develop. As a result, adult muscle fibers contain only α-fodrin (αII) and the muscle isoform of β-spectrin (βIΣ2). By contrast, other types of cells present in skeletal muscle tissue, inclu

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Dubreuil, R. R., T. J. Byers, C. T. Stewart, and D. P. Kiehart. "A beta-spectrin isoform from Drosophila (beta H) is similar in size to vertebrate dystrophin." Journal of Cell Biology 111, no. 5 (November 1, 1990): 1849–58. http://dx.doi.org/10.1083/jcb.111.5.1849.

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Spectrins are a major component of the membrane skeleton in many cell types where they are thought to contribute to cell form and membrane organization. Diversity among spectrin isoforms, especially their beta subunits, is associated with diversity in cell shape and membrane architecture. Here we describe a spectrin isoform from Drosophila that consists of a conventional alpha spectrin subunit complexed with a novel high molecular weight beta subunit (430 kD) that we term beta H. The native alpha beta H molecule binds actin filaments with high affinity and has a typical spectrin morphology exc

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Dubreuil, R. R., T. J. Byers, A. L. Sillman, D. Bar-Zvi, L. S. Goldstein, and D. Branton. "The complete sequence of Drosophila alpha-spectrin: conservation of structural domains between alpha-spectrins and alpha-actinin." Journal of Cell Biology 109, no. 5 (November 1, 1989): 2197–205. http://dx.doi.org/10.1083/jcb.109.5.2197.

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We report the complete sequence of Drosophila alpha-spectrin and show that it is similar to vertebrate nonerythroid spectrins. As in vertebrates, the alpha subunit consists of two large domains of repetitive sequence (segments 1-9 and 11-19) separated by a short nonrepetitive sequence (segment 10). The 106-residue repetitive segments are defined by a consensus sequence of 54 residues. Chicken alpha-spectrin (Wasenius, V.-M., M. Saraste, P. Salven, M. Eramaa, L. Holm, V.-P. Lehto. 1989. J. Cell Biol. 108:79-93) shares 50 of these consensus positions. Through comparison of spectrin and alpha-act

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Hanspal, M., and J. Palek. "Synthesis and assembly of membrane skeletal proteins in mammalian red cell precursors." Journal of Cell Biology 105, no. 3 (September 1, 1987): 1417–24. http://dx.doi.org/10.1083/jcb.105.3.1417.

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The synthesis of membrane skeletal proteins in avian nucleated red cells has been the subject of extensive investigation, whereas little is known about skeletal protein synthesis in bone marrow erythroblasts and peripheral blood reticulocytes in mammals. To address this question, we have isolated nucleated red cell precursors and reticulocytes from spleens and from the peripheral blood, respectively, of rats with phenylhydrazine-induced hemolytic anemia and pulse-labeled them with [35S]methionine. Pulse-labeling of nucleated red cell precursors shows that the newly synthesized alpha- and beta-

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ROTTER, Björn, Yolande KROVIARSKI, Gaël NICOLAS, Didier DHERMY, and Marie-Christine LECOMTE. "alphaII-Spectrin is an in vitro target for caspase-2, and its cleavage is regulated by calmodulin binding." Biochemical Journal 378, no. 1 (February 15, 2004): 161–68. http://dx.doi.org/10.1042/bj20030955.

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The spectrin–actin scaffold underlying the lipid bilayer is considered to participate in cell-shape stabilization and in the organization of specialized membrane subdomains. These structures are dynamic and likely to undergo frequent remodelling during changes in cell shape. Proteolysis of spectrin, which occurs during apoptosis, leads to destabilization of the scaffold. It is also one of the major processes involved in membrane remodelling. Spectrins, the main components of the membrane skeleton, are the targets for two important protease systems: m- and µ-calpains (Ca2+-activated proteases)

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Lehnert, M. E., and H. F. Lodish. "Unequal synthesis and differential degradation of alpha and beta spectrin during murine erythroid differentiation." Journal of Cell Biology 107, no. 2 (August 1, 1988): 413–26. http://dx.doi.org/10.1083/jcb.107.2.413.

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Murine erythroleukemia (MEL) cells represent a valuable system to study the biogenesis of the cytoskeleton during erythroid differentiation. When attached to fibronectin-coated dishes MEL cells induce, upon addition of DMSO, a 7-d differentiation process during which they enucleate and reach the reticulocyte stage (Patel, V. P., and H. F. Lodish. 1987. J. Cell Biol. 105:3105-3118); they accumulate band 3, spectrin, and ankyrin in amounts equivalent to those found in mature red blood cells. To follow the biosynthesis of spectrin during differentiation, membranes and cytoskeletal proteins of cel

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Kukuła, Maciej, Beata Hanus-Lorenz, Ewa Bok, Jacek Leluk та Aleksander F. Sikorski. "Proteins with Spectrin Motifs Which Do Not Belong to the Spectrin-α-Actinin- Dystrophin Family". Zeitschrift für Naturforschung C 59, № 7-8 (1 серпня 2004): 565–71. http://dx.doi.org/10.1515/znc-2004-7-821.

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AbstractUsing several consensus sequences for the 106 amino acid residue α-spectrin repeat segment as probes we searched animal sequence databases using the BLAST program in order to find proteins revealing limited, but significant similarity to spectrin. Among many spectrins and proteins from the spectrin-α-actinin-dystrophin family as well as sequences showing a rather high degree of similarity in very short stretches, we found seven homologous animal sequences of low overall similarity to spectrin but showing the presence of one or more spectrin-repeat motifs. The homology relationship of t

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McGough, Amy M., and Robert Josephs. "Electron Microscopy and image reconstruction reveal the structural basis for spectrin's elastic properties." Proceedings, annual meeting, Electron Microscopy Society of America 50, no. 1 (August 1992): 510–11. http://dx.doi.org/10.1017/s0424820100122952.

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The remarkable deformability of the erythrocyte derives in large part from the elastic properties of spectrin, the major component of the membrane skeleton. It is generally accepted that spectrin's elasticity arises from marked conformational changes which include variations in its overall length (1). In this work the structure of spectrin in partially expanded membrane skeletons was studied by electron microscopy to determine the molecular basis for spectrin's elastic properties. Spectrin molecules were analysed with respect to three features: length, conformation, and quaternary structure. T

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Patel-Hett, Sunita, Hongbei Wang, Antonija J. Begonja, Jonathan N. Thon, Eva C. Alden, Nancy J. Wandersee, Xiuli An, Narla Mohandas, John H. Hartwig, and Joseph E. Italiano. "The spectrin-based membrane skeleton stabilizes mouse megakaryocyte membrane systems and is essential for proplatelet and platelet formation." Blood 118, no. 6 (August 11, 2011): 1641–52. http://dx.doi.org/10.1182/blood-2011-01-330688.

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Abstract Megakaryocytes generate platelets by remodeling their cytoplasm first into proplatelets and then into preplatelets, which undergo fission to generate platelets. Although the functions of microtubules and actin during platelet biogenesis have been defined, the role of the spectrin cytoskeleton is unknown. We investigated the function of the spectrin-based membrane skeleton in proplatelet and platelet production in murine megakaryocytes. Electron microscopy revealed that, like circulating platelets, proplatelets have a dense membrane skeleton, the main fibrous component of which is spec

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Deng, H., J. K. Lee, L. S. Goldstein, and D. Branton. "Drosophila development requires spectrin network formation." Journal of Cell Biology 128, no. 1 (January 1, 1995): 71–79. http://dx.doi.org/10.1083/jcb.128.1.71.

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The head-end associations of spectrin give rise to tetramers and make it possible for the molecule to form networks. We analyzed the head-end associations of Drosophila spectrin in vitro and in vivo. Immunoprecipitation assays using protein fragments synthesized in vitro from recombinant DNA showed that interchain binding at the head end was mediated by segment 0-1 of alpha-spectrin and segment 18 of beta-spectrin. Point mutations equivalent to erythroid spectrin mutations that are responsible for human hemolytic anemias diminished Drosophila spectrin head-end interchain binding in vitro. To t

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Byers, T. J., R. Dubreuil, D. Branton, D. P. Kiehart, and L. S. Goldstein. "Drosophila spectrin. II. Conserved features of the alpha-subunit are revealed by analysis of cDNA clones and fusion proteins." Journal of Cell Biology 105, no. 5 (November 1, 1987): 2103–10. http://dx.doi.org/10.1083/jcb.105.5.2103.

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Drosophila alpha-spectrin cDNA sequences were isolated from a lambda gt11 expression library. These cDNA clones encode fusion proteins that include portions of the Drosophila alpha-spectrin polypeptide as shown by a number of structural and functional criteria. The fusion proteins elicited antibodies that reacted strongly with Drosophila and vertebrate alpha-spectrins and a comparison of cyanogen bromide peptide maps demonstrated a clear structural correspondence between one fusion protein and purified Drosophila alpha-spectrin. Alpha-spectrin fusion protein also displayed calcium-dependent ca

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Schneider, A., H. U. Lutz, R. Marugg, P. Gehr, and T. Seebeck. "Spectrin-like proteins in the paraflagellar rod structure of Trypanosoma brucei." Journal of Cell Science 90, no. 2 (June 1, 1988): 307–15. http://dx.doi.org/10.1242/jcs.90.2.307.

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A polyclonal, monospecific rabbit antibody to human erythrocyte spectrins cross-reacted with two sets of proteins (a doublet of 180/200K and a triplet of 67–66-65K; K = 10(3) Mr) in the parasitic protozoon Trypanosoma brucei brucei. Except for the 66K protein, the cross-reacting proteins are localized in the flagellum, on the basis of evidence from cell fractionation and immunofluorescence microscopy. Immunogold labelling and electron micrographs further revealed that the spectrin-like proteins are confined to the paraflagellar rod structure. The spectrin-like proteins with apparent molecular

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Thomas, G. H., and J. A. Williams. "Dynamic rearrangement of the spectrin membrane skeleton during the generation of epithelial polarity in Drosophila." Journal of Cell Science 112, no. 17 (September 1, 1999): 2843–52. http://dx.doi.org/10.1242/jcs.112.17.2843.

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The origin of epithelial cell polarity during development is a fundamental problem in cell biology. Central to this process is the establishment of asymmetric membrane domains that will ultimately form the apical and basolateral surfaces. The spectrin-based membrane skeleton has long been thought to participate in the generation of this asymmetry. Drosophila melanogaster contains two known (beta)-spectrin isoforms: a conventional (beta)-spectrin chain, and the novel isoform (beta)(Heavy)-spectrin. These two proteins are restricted to the basolateral and apical membrane domains, respectively. T

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Park, Sunghyouk, Michael E. Johnson, and Leslie W. M. Fung. "Nuclear magnetic resonance studies of mutations at the tetramerization region of human alpha spectrin." Blood 100, no. 1 (July 1, 2002): 283–88. http://dx.doi.org/10.1182/blood.v100.1.283.

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Abstract Many spectrin mutations that destabilize tetramer formation and lead to hereditary hemolytic anemias are located at the N-terminal region of α-spectrin, with the Arg28 position considered to be a mutation hot spot. We have introduced mutations at positions 28 and 45 into a model peptide, Spα1-156, consisting of the first 156 residues in the N-terminal region of α-spectrin (αN). The association of these α-spectrin peptides that have single amino acid replacements with a β-spectrin model peptide, consisting of the C-terminal region of β-spectrin (βC), was determined, and structural chan

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Frappier, T., F. Stetzkowski-Marden, and L. A. Pradel. "Interaction domains of neurofilament light chain and brain spectrin." Biochemical Journal 275, no. 2 (April 15, 1991): 521–27. http://dx.doi.org/10.1042/bj2750521.

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We have previously demonstrated that brain spectrin binds to the low-molecular-mass subunit of neurofilaments (NF-L) [Frappier, Regnouf & Pradel (1987) Eur. J. Biochem. 169, 651-657]. In the present study, we seek to locate their respective binding domains. In the first part we demonstrate that brain spectrin binds to a 20 kDa domain of NF-L. This domain is part of the rod domain of neurofilaments and plays a role in the polymerization process. However, the polymerization state does not seem to have any influence on the interaction. In the second part, we provide evidence that NF-L binds t

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Dubreuil, R., T. J. Byers, D. Branton, L. S. Goldstein, and D. P. Kiehart. "Drosophilia spectrin. I. Characterization of the purified protein." Journal of Cell Biology 105, no. 5 (November 1, 1987): 2095–102. http://dx.doi.org/10.1083/jcb.105.5.2095.

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We purified a protein from Drosophila S3 tissue culture cells that has many of the diagnostic features of spectrin from vertebrate organisms: (a) The protein consists of two equimolar subunits (Mr = 234 and 226 kD) that can be reversibly cross-linked into a complex composed of equal amounts of the two subunits. (b) Electron microscopy of the native molecule reveals two intertwined, elongated strands with a contour length of 180 nm. (c) Antibodies directed against vertebrate spectrin react with the Drosophila protein and, similarly, antibodies to the Drosophila protein react with vertebrate spe

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Stabach, Paul R., Ivana Simonović, Miranda A. Ranieri, Michael S. Aboodi, Thomas A. Steitz, Miljan Simonović та Jon S. Morrow. "The structure of the ankyrin-binding site of β-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties". Blood 113, № 22 (28 травня 2009): 5377–84. http://dx.doi.org/10.1182/blood-2008-10-184291.

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Spectrin and ankyrin participate in membrane organization, stability, signal transduction, and protein targeting; their interaction is critical for erythrocyte stability. Repeats 14 and 15 of βI-spectrin are crucial for ankyrin recognition, yet the way spectrin binds ankyrin while preserving its repeat structure is unknown. We have solved the crystal structure of the βI-spectrin 14,15 di-repeat unit to 2.1 Å resolution and found 14 residues critical for ankyrin binding that map to the end of the helix C of repeat 14, the linker region, and the B-C loop of repeat 15. The tilt (64°) across the 1

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Malchiodi-Albedi, F., M. Ceccarini, J. C. Winkelmann, J. S. Morrow, and T. C. Petrucci. "The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons." Journal of Cell Science 106, no. 1 (September 1, 1993): 67–78. http://dx.doi.org/10.1242/jcs.106.1.67.

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Spectrin isoforms arise from four distinct genes, three of which generate multiple alternative transcripts. With no biochemical restrictions on the assembly of alpha beta heterodimers, more than 25 distinct heterodimeric spectrin species may exist. Whether (and why) this subtle but substantial diversity is realized in any single cell is unknown. To address this question, sequence-specific antibodies to alternatively spliced regions of alpha- and beta-spectrin have been prepared. Reported here is the localization in rat cerebellar neurons at light and electron microscopic levels of an antibody

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Evans, SS, WC Wang, CC Gregorio, T. Han, and EA Repasky. "Interferon-alpha alters spectrin organization in normal and leukemic human B lymphocytes." Blood 81, no. 3 (February 1, 1993): 759–66. http://dx.doi.org/10.1182/blood.v81.3.759.bloodjournal813759.

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Interferon-alpha (IFN-alpha) regulates the growth, differentiation, and recirculation of normal and malignant B lymphocytes. In this report we examine the effects of IFN-alpha on the distribution of the cytoskeletal protein spectrin in peripheral blood B lymphocytes from normal donors and patients diagnosed with chronic lymphocytic leukemia (CLL) and hairy cell leukemia (HCL). Exposure of normal and leukemic B cells to IFN-alpha in vitro was shown by immunofluorescence microscopy to cause a dose-dependent increase in the percentage of cells containing discrete focal accumulations of spectrin,

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Evans, SS, WC Wang, CC Gregorio, T. Han, and EA Repasky. "Interferon-alpha alters spectrin organization in normal and leukemic human B lymphocytes." Blood 81, no. 3 (February 1, 1993): 759–66. http://dx.doi.org/10.1182/blood.v81.3.759.759.

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Abstract Interferon-alpha (IFN-alpha) regulates the growth, differentiation, and recirculation of normal and malignant B lymphocytes. In this report we examine the effects of IFN-alpha on the distribution of the cytoskeletal protein spectrin in peripheral blood B lymphocytes from normal donors and patients diagnosed with chronic lymphocytic leukemia (CLL) and hairy cell leukemia (HCL). Exposure of normal and leukemic B cells to IFN-alpha in vitro was shown by immunofluorescence microscopy to cause a dose-dependent increase in the percentage of cells containing discrete focal accumulations of s

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Lambert, Muriel W. "Spectrin and its interacting partners in nuclear structure and function." Experimental Biology and Medicine 243, no. 6 (March 2018): 507–24. http://dx.doi.org/10.1177/1535370218763563.

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Nonerythroid αII-spectrin is a structural protein whose roles in the nucleus have just begun to be explored. αII-spectrin is an important component of the nucleoskelelton and has both structural and non-structural functions. Its best known role is in repair of DNA ICLs both in genomic and telomeric DNA. αII-spectrin aids in the recruitment of repair proteins to sites of damage and a proposed mechanism of action is presented. It interacts with a number of different groups of proteins in the nucleus, indicating it has roles in additional cellular functions. αII-spectrin, in its structural role,

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Wolgast, Lucia R., Linda A. Cannizzarro, K. H. Ramesh, Xiaonan Xue, Dan Wang, Pritish K. Bhattacharyya, Jerald Z. Gong, et al. "Spectrin Isoforms." American Journal of Clinical Pathology 136, no. 2 (August 2011): 300–308. http://dx.doi.org/10.1309/ajcpsa5rnm9igfjf.

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Franck, Paul Hubert Frans, Cobie Postma, Marjan Veuger, Pierre Wijermans та Frans A. Kuypers. "A Family with Hereditary Elliptocytosis: Variable Clinical Severity Caused by Three Mutations in the α-Spectrin Gene",. Blood 118, № 21 (18 листопада 2011): 3167. http://dx.doi.org/10.1182/blood.v118.21.3167.3167.

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Abstract Abstract 3167 Introduction The membrane of erythrocytes is composed of a bilayer of phospholipids and cholesterol. It is strengthened by a membraneskeleton consisting of the proteins spectrin, ankyrin, pallidin, band 3 and band 4.1. Hereditary elliptocytosis (HE) is caused by mutations in the spectrin protein, resulting in a typical elliptocytic shape. These cells have a decreased deformability and a shortened lifespan. Most mutations in HE are located in the head to head self association site of the α- and β dimers of spectrin. HE Patients with heterozygous mutations in α spectrin sh

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Yang, Yang, Yasuhiro Ogawa, Kristian L. Hedstrom та Matthew N. Rasband. "βIV spectrin is recruited to axon initial segments and nodes of Ranvier by ankyrinG". Journal of Cell Biology 176, № 4 (5 лютого 2007): 509–19. http://dx.doi.org/10.1083/jcb.200610128.

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High densities of ion channels at axon initial segments (AISs) and nodes of Ranvier are required for initiation, propagation, and modulation of action potentials in axons. The organization of these membrane domains depends on a specialized cytoskeleton consisting of two submembranous cytoskeletal and scaffolding proteins, ankyrinG (ankG) and βIV spectrin. However, it is not known which of these proteins is the principal organizer, or if the mechanisms governing formation of the cytoskeleton at the AIS also apply to nodes. We identify a distinct protein domain in βIV spectrin required for its l

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Lorenzo, Damaris N., Alexandra Badea, Ruobo Zhou, Peter J. Mohler, Xiaowei Zhuang та Vann Bennett. "βII-spectrin promotes mouse brain connectivity through stabilizing axonal plasma membranes and enabling axonal organelle transport". Proceedings of the National Academy of Sciences 116, № 31 (17 червня 2019): 15686–95. http://dx.doi.org/10.1073/pnas.1820649116.

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βII-spectrin is the generally expressed member of the β-spectrin family of elongated polypeptides that form micrometer-scale networks associated with plasma membranes. We addressed in vivo functions of βII-spectrin in neurons by knockout of βII-spectrin in mouse neural progenitors. βII-spectrin deficiency caused severe defects in long-range axonal connectivity and axonal degeneration. βII-spectrin–null neurons exhibited reduced axon growth, loss of actin–spectrin-based periodic membrane skeleton, and impaired bidirectional axonal transport of synaptic cargo. We found that βII-spectrin associat

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Matsushita, Hirokazu, Matthew Vesely, Ravindra Uppaluri, and Robert Schreiber. "Antigen immunoselection as a mechanism of cancer immunoediting (165.3)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 165.3. http://dx.doi.org/10.4049/jimmunol.186.supp.165.3.

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Abstract Cancer immunoediting is the process wherein the immune system not only protects against tumor development but also promotes outgrowth of tumors with reduced immunogenicity. Although we and others identified several key immune components that participate in this process, we know very little about the targets of cancer immunoediting. In this study we used a highly immunogenic methylcholanthrene induced sarcoma cell line (d42m1) to ask whether tumor antigens can be immunoediting targets. Like most unedited MCA sarcomas, d42m1 cells form tumors when transplanted into immunodeficient mice

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Berghs, Stanny, Diego Aggujaro, Ronald Dirkx, Elena Maksimova, Paul Stabach, Jean-Michel Hermel, Jian-Ping Zhang та ін. "βiv Spectrin, a New Spectrin Localized at Axon Initial Segments and Nodes of Ranvier in the Central and Peripheral Nervous System". Journal of Cell Biology 151, № 5 (27 листопада 2000): 985–1002. http://dx.doi.org/10.1083/jcb.151.5.985.

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We report the identification of βIV spectrin, a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. The βIV spectrin gene is located on human and mouse chromosomes 19q13.13 and 7b2, respectively. Alternative splicing of βIV spectrin generates at least four distinct isoforms, numbered βIVΣ1–βIVΣ4 spectrin. The longest isoform (βIVΣ1 spectrin) includes an actin-binding domain, followed by 17 spectrin repeats, a specific domain in which the amino acid sequence ERQES is repeated four times, several putative SH3-binding sites and a pleckstrin homology

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40

Higgs, Henry N. "Spectres of spectrin: molecular modeling and hemolytic disease." Trends in Biochemical Sciences 26, no. 12 (December 2001): 702. http://dx.doi.org/10.1016/s0968-0004(01)02004-7.

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41

Hanspal, M., JS Hanspal, KE Sahr, E. Fibach, J. Nachman, and J. Palek. "Molecular basis of spectrin deficiency in hereditary pyropoikilocytosis." Blood 82, no. 5 (September 1, 1993): 1652–60. http://dx.doi.org/10.1182/blood.v82.5.1652.1652.

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Abstract Hereditary pyropoikilocytosis (HPP) is a recessively inherited hemolytic anemia characterized by severe poikilocytosis and red blood cell fragmentation. HPP red blood cells are partially deficient in spectrin and contain a mutant alpha or beta-spectrin that is defective in terms of spectrin self-association. Although the nature of the latter defect has been studied in considerable detail and many mutations of alpha-spectrin and beta spectrin have been identified, the molecular basis of spectrin deficiency is unknown. Here we report two mechanisms underlying spectrin deficiency in HPP.

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Hanspal, M., JS Hanspal, KE Sahr, E. Fibach, J. Nachman, and J. Palek. "Molecular basis of spectrin deficiency in hereditary pyropoikilocytosis." Blood 82, no. 5 (September 1, 1993): 1652–60. http://dx.doi.org/10.1182/blood.v82.5.1652.bloodjournal8251652.

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Hereditary pyropoikilocytosis (HPP) is a recessively inherited hemolytic anemia characterized by severe poikilocytosis and red blood cell fragmentation. HPP red blood cells are partially deficient in spectrin and contain a mutant alpha or beta-spectrin that is defective in terms of spectrin self-association. Although the nature of the latter defect has been studied in considerable detail and many mutations of alpha-spectrin and beta spectrin have been identified, the molecular basis of spectrin deficiency is unknown. Here we report two mechanisms underlying spectrin deficiency in HPP. The firs

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Leshchyns'ka, Iryna, Vladimir Sytnyk, Jon S. Morrow та Melitta Schachner. "Neural cell adhesion molecule (NCAM) association with PKCβ2 via βI spectrin is implicated in NCAM-mediated neurite outgrowth". Journal of Cell Biology 161, № 3 (12 травня 2003): 625–39. http://dx.doi.org/10.1083/jcb.200303020.

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In hippocampal neurons and transfected CHO cells, neural cell adhesion molecule (NCAM) 120, NCAM140, and NCAM180 form Triton X-100–insoluble complexes with βI spectrin. Heteromeric spectrin (αIβI) binds to the intracellular domain of NCAM180, and isolated spectrin subunits bind to both NCAM180 and NCAM140, as does the βI spectrin fragment encompassing second and third spectrin repeats (βI2–3). In NCAM120-transfected cells, βI spectrin is detectable predominantly in lipid rafts. Treatment of cells with methyl-β-cyclodextrin disrupts the NCAM120–spectrin complex, implicating lipid rafts as a pla

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Mazock, G. Harper, Amlan Das, Christine Base та Ronald R. Dubreuil. "Transgene Rescue Identifies an Essential Function for Drosophila β Spectrin in the Nervous System and a Selective Requirement for Ankyrin-2–binding Activity". Molecular Biology of the Cell 21, № 16 (15 серпня 2010): 2860–68. http://dx.doi.org/10.1091/mbc.e10-03-0180.

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The protein spectrin is ubiquitous in animal cells and is believed to play important roles in cell shape and membrane stability, cell polarity, and endomembrane traffic. Experiments here were undertaken to identify sites of essential β spectrin function in Drosophila and to determine whether spectrin and ankyrin function are strictly linked to one another. The Gal4-UAS system was used to drive tissue-specific overexpression of a β spectrin transgene or to knock down β spectrin expression with dsRNA. The results show that 1) overexpression of β spectrin in most of the cell types studied was let

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45

Hulsmeier, J., J. Pielage, C. Rickert, G. M. Technau, C. Klambt, and T. Stork. "Distinct functions of -Spectrin and -Spectrin during axonal pathfinding." Development 134, no. 4 (January 10, 2007): 713–22. http://dx.doi.org/10.1242/dev.02758.

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46

Coetzer, T., J. Lawler, JT Prchal, and J. Palek. "Molecular determinants of clinical expression of hereditary elliptocytosis and pyropoikilocytosis." Blood 70, no. 3 (September 1, 1987): 766–72. http://dx.doi.org/10.1182/blood.v70.3.766.766.

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Abstract The clinical severity of common hereditary elliptocytosis (HE) is highly variable, ranging from an asymptomatic carrier state to a severe hemolytic anemia. To elucidate the molecular basis of this variable clinical expression, we evaluated 56 subjects from 24 HE kindred, who carry alpha spectrin mutants characterized by a spectrin dimer (SpD) self-association defect related to a structural abnormality of the alpha I domain of spectrin. Twenty-nine subjects had common HE, 13 subjects have a closely related disorder, hereditary pyropoikilocytosis (HPP), and 14 are asymptomatic carriers.

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47

Coetzer, T., J. Lawler, JT Prchal, and J. Palek. "Molecular determinants of clinical expression of hereditary elliptocytosis and pyropoikilocytosis." Blood 70, no. 3 (September 1, 1987): 766–72. http://dx.doi.org/10.1182/blood.v70.3.766.bloodjournal703766.

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The clinical severity of common hereditary elliptocytosis (HE) is highly variable, ranging from an asymptomatic carrier state to a severe hemolytic anemia. To elucidate the molecular basis of this variable clinical expression, we evaluated 56 subjects from 24 HE kindred, who carry alpha spectrin mutants characterized by a spectrin dimer (SpD) self-association defect related to a structural abnormality of the alpha I domain of spectrin. Twenty-nine subjects had common HE, 13 subjects have a closely related disorder, hereditary pyropoikilocytosis (HPP), and 14 are asymptomatic carriers. We compa

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48

Li, Donghai. "Role of Spectrin in Endocytosis." Cells 11, no. 15 (August 8, 2022): 2459. http://dx.doi.org/10.3390/cells11152459.

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Cytoskeletal spectrin is found in (non)erythroid cells. Eukaryotic endocytosis takes place for internalizing cargos from extracellular milieu. The role of spectrin in endocytosis still remains poorly understood. Here, I summarize current knowledge of spectrin function, spectrin-based cytoskeleton and endocytosis of erythrocytes, and highlight how spectrin contributes to endocytosis and working models in different types of cells. From an evolutionary viewpoint, I discuss spectrin and endocytosis in a range of organisms, particularly in plants and yeast where spectrin is absent. Together, the ro

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49

Cohen, AM, SC Liu, LH Derick, and J. Palek. "Ultrastructural studies of the interaction of spectrin with phosphatidylserine liposomes." Blood 68, no. 4 (October 1, 1986): 920–26. http://dx.doi.org/10.1182/blood.v68.4.920.920.

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Abstract Spectrin was shown previously to interact with phosphatidylserine and phosphatidylethanolamine, which are preferentially localized in the inner half of the membrane lipid bilayer, but this interaction is not well characterized. In the present study we used electron microscopy of rotary-shadowed platinum replicas of spectrin dimer-phosphatidylserine complexes to study the interaction of spectrin with phosphatidylserine vesicles. At a spectrin concentration of 0.6 mg/mL, 60% of spectrin dimers were associated with phosphatidylserine vesicles and at a spectrin concentration of 1.2 mg/mL,

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50

Cohen, AM, SC Liu, LH Derick, and J. Palek. "Ultrastructural studies of the interaction of spectrin with phosphatidylserine liposomes." Blood 68, no. 4 (October 1, 1986): 920–26. http://dx.doi.org/10.1182/blood.v68.4.920.bloodjournal684920.

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Spectrin was shown previously to interact with phosphatidylserine and phosphatidylethanolamine, which are preferentially localized in the inner half of the membrane lipid bilayer, but this interaction is not well characterized. In the present study we used electron microscopy of rotary-shadowed platinum replicas of spectrin dimer-phosphatidylserine complexes to study the interaction of spectrin with phosphatidylserine vesicles. At a spectrin concentration of 0.6 mg/mL, 60% of spectrin dimers were associated with phosphatidylserine vesicles and at a spectrin concentration of 1.2 mg/mL, some ves

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