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Journal articles on the topic 'Spectrine'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 May 2024

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1

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 (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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2

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 (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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3

Delaunay, J., R. Wilmotte, N. Alloisio та J. Maréchal. "L'allèle αLELY, un allèle tranquille, mais dangereux, du gène α-spectrine érythroïde". médecine/sciences 11, № 5 (1995): 752. http://dx.doi.org/10.4267/10608/2272.

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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 (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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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 (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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6

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 (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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7

Leto, T. L., D. Fortugno-Erikson, D. Barton, et al. "Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species." Molecular and Cellular Biology 8, no. 1 (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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8

Leto, T. L., D. Fortugno-Erikson, D. Barton, et al. "Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species." Molecular and Cellular Biology 8, no. 1 (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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9

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 (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 (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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11

Nicolas, Gaël, Catherine M. Fournier, Colette Galand, et al. "Tyrosine Phosphorylation Regulates Alpha II Spectrin Cleavage by Calpain." Molecular and Cellular Biology 22, no. 10 (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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Hanspal, M., and J. Palek. "Synthesis and assembly of membrane skeletal proteins in mammalian red cell precursors." Journal of Cell Biology 105, no. 3 (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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Baines, Anthony J. "Evolution of spectrin function in cytoskeletal and membrane networks." Biochemical Society Transactions 37, no. 4 (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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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 (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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15

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 (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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16

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 (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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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 (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, 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 (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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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 (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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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 (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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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 (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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Patel-Hett, Sunita, Hongbei Wang, Antonija J. Begonja, et al. "The spectrin-based membrane skeleton stabilizes mouse megakaryocyte membrane systems and is essential for proplatelet and platelet formation." Blood 118, no. 6 (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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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 (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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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 (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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Frappier, T., F. Stetzkowski-Marden, and L. A. Pradel. "Interaction domains of neurofilament light chain and brain spectrin." Biochemical Journal 275, no. 2 (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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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 (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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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 (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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Winkelmann, JC, and BG Forget. "Erythroid and nonerythroid spectrins." Blood 81, no. 12 (1993): 3173–85. http://dx.doi.org/10.1182/blood.v81.12.3173.3173.

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Abstract Recent developments have contributed important information to understanding the role of spectrins in the RBC membrane skeleton and nonerythroid cells. Many questions can now be framed, informed by structural knowledge of various spectrin subunit types and alternatively spliced variants, that previously could not have been addressed. Their solution in the coming years will likely lead to further advances with direct relevance to biology and medicine.

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Winkelmann, JC, and BG Forget. "Erythroid and nonerythroid spectrins." Blood 81, no. 12 (1993): 3173–85. http://dx.doi.org/10.1182/blood.v81.12.3173.bloodjournal81123173.

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Recent developments have contributed important information to understanding the role of spectrins in the RBC membrane skeleton and nonerythroid cells. Many questions can now be framed, informed by structural knowledge of various spectrin subunit types and alternatively spliced variants, that previously could not have been addressed. Their solution in the coming years will likely lead to further advances with direct relevance to biology and medicine.

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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 (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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Deng, H., J. K. Lee, L. S. Goldstein, and D. Branton. "Drosophila development requires spectrin network formation." Journal of Cell Biology 128, no. 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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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 (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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Stabach, Paul R., Ivana Simonović, Miranda A. Ranieri та ін. "The structure of the ankyrin-binding site of β-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties". Blood 113, № 22 (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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Lambert, Muriel W. "Spectrin and its interacting partners in nuclear structure and function." Experimental Biology and Medicine 243, no. 6 (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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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 (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 (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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37

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 (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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Gough, Lisa Lucio, Jun Fan, Stephen Chu, Shawn Winnick, and Kenneth A. Beck. "Golgi Localization of Syne-1." Molecular Biology of the Cell 14, no. 6 (2003): 2410–24. http://dx.doi.org/10.1091/mbc.e02-07-0446.

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We have previously identified a Golgi-localized spectrin isoform by using an antibody to the β-subunit of erythrocyte spectrin. In this study, we show that a screen of a λgt11 expression library resulted in the isolation of an ∼5-kb partial cDNA from a Madin-Darby bovine kidney (MDBK) cell line, which encoded a polypeptide of 1697 amino acids with low, but detectable, sequence homology to spectrin (37%). A blast search revealed that this clone overlaps with the 5′ end of a recently identified spectrin family member Syne-1B/Nesprin-1β, an alternately transcribed gene with muscle-specific forms

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39

Liao, E. C., B. H. Paw, L. L. Peters, et al. "Hereditary spherocytosis in zebrafish riesling illustrates evolution of erythroid beta-spectrin structure, and function in red cell morphogenesis and membrane stability." Development 127, no. 23 (2000): 5123–32. http://dx.doi.org/10.1242/dev.127.23.5123.

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Spectrins are key cytoskeleton proteins with roles in membrane integrity, cell morphology, organelle transport and cell polarity of varied cell types during development. Defects in erythroid spectrins in humans result in congenital hemolytic anemias with altered red cell morphology. Although well characterized in mammals and invertebrates, analysis of the structure and function of non-mammalian vertebrate spectrins has been lacking. The zebrafish riesling (ris) suffers from profound anemia, where the developing red cells fail to assume terminally differentiated erythroid morphology. Using comp

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Hayes, N. V., C. Scott, E. Heerkens, et al. "Identification of a novel C-terminal variant of beta II spectrin: two isoforms of beta II spectrin have distinct intracellular locations and activities." Journal of Cell Science 113, no. 11 (2000): 2023–34. http://dx.doi.org/10.1242/jcs.113.11.2023.

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It is established that variations in the structure and activities of betaI spectrin are mediated by differential mRNA splicing. The two betaI spectrin splice forms so far identified have either long or short C-terminal regions. Are analogous mechanisms likely to mediate regulation of betaII spectrins? Thus far, only a long form of betaII spectrin is reported in the literature. Five human expressed sequence tags indicated the existence of a short splice variant of betaII spectrin. The occurrence and DNA sequence of the short C-terminal variant was confirmed by analysis of human and rat cDNA. Th

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Mařík, T., B. Bíbr, M. Kselíková, K. Dobrovský, J. Kolínská, and J. Lener. "Structural analogy among mammalian spectrins and spectrin-like proteins revealed by molybdenum labeling." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 86, no. 3 (1987): 531–35. http://dx.doi.org/10.1016/0305-0491(87)90443-3.

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Berkani, M., and A. Ouahab. "Théorème de l’application spectrale pour le spectre essentiel quasi-Fredholm." Proceedings of the American Mathematical Society 125, no. 3 (1997): 763–74. http://dx.doi.org/10.1090/s0002-9939-97-03431-x.

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Idziorek, Thierry, Julie Cazareth, Catherine Blanc, Nathalie Jouy, Pierre Bourdely, and Aurélien Corneau. "Que la lumière soit. Et si ce n’était plus seulement vrai !" médecine/sciences 34, no. 5 (2018): 439–47. http://dx.doi.org/10.1051/medsci/20183405017.

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Ces dernières années ont vu une progression importante des capacités des nouveaux appareils de cytométrie. Deux sauts technologiques ont été récemment franchis avec la cytométrie couplée à la spectrométrie de masse, dans laquelle les fluorochromes ont été remplacés par des métaux rares non radioactifs de la famille des lanthanides et la cytométrie spectrale qui collecte les photons sur le spectre visible. Dans cette revue, nous décrivons schématiquement la cytométrie en flux conventionnelle et ces deux technologies ainsi que leurs avantages et adaptabilités et leurs inconvénients.

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Chierchia, Loredana, Margherita Tussellino, Domenico Guarino, et al. "Cytoskeletal proteins associate with components of the ribosomal maturation and translation apparatus in Xenopus stage I oocytes." Zygote 23, no. 5 (2014): 669–82. http://dx.doi.org/10.1017/s0967199414000409.

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SummaryActin-based cytoskeleton (CSK) and microtubules may bind to RNAs and related molecules implicated in translation. However, many questions remain to be answered regarding the role of cytoskeletal components in supporting the proteins involved in steps in the maturation and translation processes. Here, we performed co-immunoprecipitation and immunofluorescence to examine the association between spectrins, keratins and tubulin and proteins involved in 60S ribosomal maturation and translation in Xenopus stage I oocytes, including ribosomal rpl10, eukaryotic initiation factor 6 (Eif6), thesa

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Pain, Jean-Christophe. "L’hélio-sismologie et l’énigme de l’opacité du fer." Reflets de la physique, no. 58 (June 2018): 10–15. http://dx.doi.org/10.1051/refdp/201858010.

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La mesure du spectre de pulsations d’une étoile permet d’obtenir des informations sur les processus physiques qui régissent sa structure et son évolution. La révision récente des abondances chimiques solaires entraîne un désaccord entre le modèle stellaire standard et les mesures d’hélio-sismologie. L’opacité du fer a été mesurée en laboratoire, dans des conditions proches de celles de l’interface entre les zones radiative et convective du Soleil. Les opacités déduites des mesures sont, dans une gamme spectrale allant de 7 à 12,7 Å, de 30 à 400 % supérieures aux calculs, ce qui tend à réconcil

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Hong, Yeonsun, and Minsoo Kim. "Abstract A10: In vivo CRISPR screen reveals how to drive therapeutic T cell function to solid tumors." Cancer Immunology Research 10, no. 12_Supplement (2022): A10. http://dx.doi.org/10.1158/2326-6074.tumimm22-a10.

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Abstract Chimeric antigen receptor (CAR)-T cell therapy is emerging as a promising option for cancer immunotherapy. Although CAR-T cell therapy has excellent efficacy in the treatment of hematologic malignancies, it has largely failed in patients with solid tumors due to several problems, such as homing and trafficking. Here, we performed an in vivo targeted CRISPR-Cas9 screens to identify a molecular regulator of off-target trafficking of CAR-T cells, and identified ST3 b-galactoside a-2,3-sialyltransferase1 (St3gal1) as a major negative factor of CAR-T cells migration. Analysis of Maackia am

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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 (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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Berghs, Stanny, Diego Aggujaro, Ronald Dirkx 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 (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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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 (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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50

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 (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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