Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton

Morrow, Jon S.; Rimm, David L.; Kennedy, Scott P.; Cianci, Carol D.; Sinard, John H.; Weed, Scott A.

doi:10.1002/cphy.cp140111

Cited by 36 publications

(53 citation statements)

References 506 publications

(393 reference statements)

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“…[1][2][3]. Formation of the membrane skeleton involves multiple protein-protein interactions among integral membrane proteins.…”

Section: From the New York State Institute For Basic Research In Devementioning

confidence: 99%

Identification of a Candidate Human Spectrin Src Homology 3 Domain-binding Protein Suggests a General Mechanism of Association of Tyrosine Kinases with the Spectrin-based Membrane Skeleton

Ziemnicka-Kotula

et al. 1998

Journal of Biological Chemistry

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Erythroid spectrin is the predominant component of the twodimensional protein network called the membrane skeleton, underlying the lipid bilayer of red cells (for recent reviews, seeRefs. 1-3). Formation of the membrane skeleton involves multiple protein-protein interactions among integral membrane proteins. Interactions of spectrin with other membrane proteins such as ankyrin, protein 4.1, and adducin provide a linkage of spectrin either to the plasma membrane or among spectrin tetramers. Many hereditary anemia mutations affect interactions of these integral membrane proteins, resulting in increased fragility and shortened lifespan of erythrocytes. In hereditary elliptocytosis and pyropoikilocytosis, the mutations have been localized in the ␣-and ␤-subunits of spectrin (reviewed in Refs. 4 and 5). Many of these proteins, including spectrin, which were first identified in red cells, have isoforms expressed in nonerythroid cells, but the structure and regulatory processes of the nonerythroid membrane skeleton are less well understood (reviewed in Refs. 1-3, 6, and 7). Functional differences between the membranes of erythroid and nonerythroid cells argue against the simple erythrocyte model of the membrane skeleton. Major differences between the erythroid model and other cells include differences in the expression of spectrin (8 -11) and ankyrin isoforms (12-15) (reviewed in Ref.16), interactions of spectrin and ankyrin with additional proteins (17-21), localization of spectrin in the cytoplasm as well as in the plasma membrane (10,11,22), and the potential for dramatic rearrangements of spectrin's cellular location (23, 24) (reviewed in Refs. 2 and 7).Several studies have demonstrated that both erythroid and nonerythroid spectrins are expressed in brain tissue (8 -11, 25). Neuronal compartmentalization of brain spectrin isoforms into axons and presynaptic terminals (nonerythroid spectrin) and into cell bodies and dendrites (erythroid spectrin) (10, 25) suggests that brain spectrin isoforms may perform related but distinct functions in neuronal cells. It has been suggested that nonerythroid spectrin performs a more general, constitutive role, while erythroid spectrin takes part in more specialized activities of differentiated cells (26). The ␣-subunit of erythroid spectrin, ␣I (27), 1 and the ␣-subunit of nonerythroid spectrin, ␣II (28, 29), each contains a unique SH3 2 domain. Distinct protein interactions are likely to involve these domains, and they may be important for specific distribution and specialized roles of brain spectrin isoforms.

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“…[1][2][3]. Formation of the membrane skeleton involves multiple protein-protein interactions among integral membrane proteins.…”

Section: From the New York State Institute For Basic Research In Devementioning

confidence: 99%

Identification of a Candidate Human Spectrin Src Homology 3 Domain-binding Protein Suggests a General Mechanism of Association of Tyrosine Kinases with the Spectrin-based Membrane Skeleton

Ziemnicka-Kotula

et al. 1998

Journal of Biological Chemistry

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“…Spectrin, the most abundant protein of the erythrocyte membrane skeleton, is composed of two structurally similar but nonidentical proteins, ␣-and ␤-spectrin, encoded by separate genes (1,2). ␣-and ␤-spectrin are composed primarily of homologous 106-amino acid repeats that fold into three antiparallel ␣-helices connected by short nonhelical segments (3)(4)(5)(6)(7).…”

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“…␣-and ␤-spectrin combine to form heterodimers, which in turn self-associate to form tetramers and higher order oligomers to form a lattice-like structure that is critical for erythrocyte membrane stability, as well as erythrocyte shape and deformability (8 -12). In the red cell, spectrin maintains cellular shape, regulates the lateral mobility of integral membrane proteins, and provides structural support for the lipid bilayer (2,13). Quantitative and qualitative disorders of ␣-spectrin have been associated with abnormalities of erythrocyte shape including hereditary spherocytosis, elliptocytosis, and pyropoikilocytosis (12, 14 -19).…”

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Erythroid Expression of the Human α-Spectrin Gene Promoter Is Mediated by GATA-1- and NF-E2-binding Proteins

Boulanger¹,

Sabatino²,

Wong³

et al. 2002

Journal of Biological Chemistry

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␣-Spectrin is a highly expressed membrane protein critical for the flexibility and stability of the erythrocyte. Qualitative and quantitative defects of ␣-spectrin are present in the erythrocytes of many patients with abnormalities of red blood cell shape including hereditary spherocytosis and elliptocytosis. We wished to determine the regulatory elements that determine the erythroid-specific expression of the ␣-spectrin gene. We mapped the 5 end of the ␣-spectrin erythroid cDNA and cloned the 5 flanking genomic DNA containing the putative ␣-spectrin gene promoter. Using transfection of promoter/reporter plasmids in human tissue culture cell lines, in vitro DNase I footprinting analyses, and gel mobility shift assays, an ␣-spectrin gene erythroid promoter with binding sites for GATA-1-and NF-E2-related proteins was identified. Both binding sites were required for full promoter activity. In transgenic mice, a reporter gene directed by the ␣-spectrin promoter was expressed in yolk sac, fetal liver, and erythroid cells of bone marrow but not adult reticulocytes. No expression of the reporter gene was detected in nonerythroid tissues. We conclude that this ␣-spectrin gene promoter contains the sequences necessary for low level expression in erythroid progenitor cells.

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“…First characterized in erythrocytes (1), spectrin maintains the structural integrity of the red blood cell membrane and is defective in several inherited hemolytic anemias (2). Isoforms of spectrin probably are present in all cells, where they help to establish and maintain an organized distribution of membrane proteins (3). Recently, spectrin homologues and their binding partners have been identified in association with several intracellular organelles and have been found to participate in membrane protein sorting and organelle transport (4)(5)(6)(7)(8)(9)(10)(11).…”

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A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles

Stankewich

Tse

Peters

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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104

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Spectrin is an important structural component of the plasma membrane skeleton. Heretoforeunidentified isoforms of spectrin also associate with Golgi and other organelles. We have discovered another member of the ␤-spectrin gene family by homology searches of the GenBank databases and by 5 rapid amplification of cDNA ends of human brain cDNAs. Collectively, 7,938 nucleotides of contiguous clones are predicted to encode a 271,294-Da protein, called ␤III spectrin, with conserved actin-, protein 4.1-, and ankyrin-binding domains, membrane association domains 1 and 2, a spectrin dimer self-association site, and a pleckstrinhomology domain. ␤III spectrin transcripts are concentrated in the brain and present in the kidneys, liver, and testes and the prostate, pituitary, adrenal, and salivary glands. All of the tested tissues contain major 9.0-kb and minor 11.3-kb transcripts. The human ␤III spectrin gene (SPTBN2) maps to chromosome 11q13 and the mouse gene (Spnb3) maps to a syntenic region close to the centromere on chromosome 19. Indirect immunof luorescence studies of cultured cells using antisera specific to human ␤III spectrin reveal a Golgiassociated and punctate cytoplasmic vesicle-like distribution, suggesting that ␤III spectrin associates with intracellular organelles. This distribution overlaps that of several Golgi and vesicle markers, including mannosidase II, p58, transGolgi network (TGN)38, and ␤-COP and is distinct from the endoplasmic reticulum markers calnexin and Bip. Liver Golgi membranes and other vesicular compartment markers cosediment in vitro with ␤III spectrin. ␤III spectrin thus constitutes a major component of the Golgi and vesicular membrane skeletons.

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Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton

Abstract: The sections in this article are: The Red Cell Membrane Skeleton How Does the Spectrin Membrane Skeleton Stabilize the Red Cell? The Trilayer Couple—Spectrin as A Membrane Organizer Components of the Erythrocyte Membrane Skeleton Spectrin Actin Ankyrin … Show more

Cited by 36 publications

References 506 publications

Identification of a Candidate Human Spectrin Src Homology 3 Domain-binding Protein Suggests a General Mechanism of Association of Tyrosine Kinases with the Spectrin-based Membrane Skeleton

Identification of a Candidate Human Spectrin Src Homology 3 Domain-binding Protein Suggests a General Mechanism of Association of Tyrosine Kinases with the Spectrin-based Membrane Skeleton

Erythroid Expression of the Human α-Spectrin Gene Promoter Is Mediated by GATA-1- and NF-E2-binding Proteins

A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles

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