Brain spectrin: Of mice and men

Goodman, Steven R.; Zimmer, Warren E.; Clark, Mary Blair; Zagon, Ian S.; Barker, Jane E.; Bloom, Michael L.

doi:10.1016/0361-9230(94)00264-2

Cited by 122 publications

(145 citation statements)

References 113 publications

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“…The C-terminal domains of erythroid and nonerythroid b-spectrins do not conform to the spectrin repeat motif, and are involved, together with the N-terminal domain of the a-subunit, in spectrin dimer association (Goodman et al, , 1995Tse et al, 1990). The strong similarity of C-terminal domains of erythroid and nonerythroid b-spectrins may account for the observed di erence in spectrin tetramer formation and stability between erythroid and nonerythroid subunits.…”

Section: Discussionmentioning

confidence: 97%

“…They include Spna-1 (a-erythrocyte spectrin or aSpIS1, which has been mapped to chromosome 1 both in mouse and human), Spna-2 (a-nonerythroid spectrin or aSpIIS1, which has been mapped to chromosome 2 in mouse and chromosome 9 in human), Spnb-1 (b-erythrocyte spectrin or bSpIS1/ bSpIS2, mapped to chromosome 12 in mouse and chromosome 14 in human), and Spnb-2 (b-nonerythroid spectrin or bSpIIS1, mapped to chromosome 11 in mouse and chromosome 2 in human) (Goodman et al, 1995).…”

Section: Elf3 Maps To Mouse Chromosome 11mentioning

confidence: 99%

“…These properties allow the membrane skeleton to facilitate the formation of distinct membrane domains, de®ning the role of spectrins as a membrane protein-sorting machine (Beck and Nelson, 1996). For instance, an isoform of spectrin (aSpIS*/bSpIS2) homologous to the erythroid spectrin localizes to the neuronal cell bodies and dendritic processes of granule cells as well as other classes of neurons, whereas another isoform (aSpIIbS1/bSpIIS1) distinct from the erythroid spectrins localizes to the axonal plasma membrane and presynaptic terminals (Goodman et al, 1995). In polarized Madin-Darby canine kidney (MDCK) epithelial cells, the distribution of a nonerythroid isoform of spectrin is restricted to the basolateral plasma membrane domain .…”

Section: Plasma Membranes Of Polarized Cells and Spectrins As A Membrmentioning

confidence: 99%

“…Spectrins comprise a-and b-subunits approximately 200 nm in length that are cross-linked by short actin ®laments at junctional complexes, which include protein 4.1, 4.9, myosin, tropomyosin, PS5 and adducin, etc. To date, the best characterized spectrins are erythrocytic and brain spectrin (Goodman et al, 1995;Riederer et al, 1986). The subunits of erythrocyte spectrin have molecular masses of 240 kDa (a-subunit) and 220 kDa (b-subunit), whereas those of brain spectrin (also called fodrin) are 240 and 235 kDa (Goodman et al, 1981;Bennett et al, 1982;Gallagher and Forget, 1993).…”

Section: Introductionmentioning

confidence: 99%

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Elf3 encodes a novel 200-kD β-spectrin: role in liver development

et al. 1999

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b-spectrins are crucial for the maintenance of cell shape, the establishment of cell polarity, and the formation of distinct membrane domains. Our strategy for identifying genes important for hepatocyte polarity has been to utilize subtractive hybridization of early embryonic mouse cDNA liver libraries. As a result, we have cloned three isoforms of a novel b-spectrin elf (embryonic liver b-fodrin), and here we report the analysis of elf3, the longest isoform (8172 nt). ELF3 comprises 2154 residues with an overall similarity of 89.0% and 95.3% to mouse b-spectrin (bSpIIS1) at the nucleotide and amino acid level, respectively. ELF3 is characterized by an actinbinding domain, a long repeat domain, and a short regulatory domain remarkable for the absence of a PH domain. Linkage analysis reveals that elf3 maps to mouse chromosome 11 between D11Bir6 and D11Xrf477, a di erent chromosomal locus from that of the other four spectrin genes. Northern blot analysis utilizing an elf3 3'-UTR probe demonstrates an abundant 9.0-kb transcript in brain, liver, and heart tissues. Western blot with a polyclonal antibody against ELF identi®es a 200 kD protein in mouse liver, brain, kidney, and heart tissues. Immunohistochemical studies demonstrate ELF labeling of the basolateral or sinusoidal membranes surface as well as a granular cytoplasmic pattern in hepatocytes. Antisense studies utilizing cultured liver explants show a vital role of elf3 in hepatocyte di erentiation and intrahepatic bile duct formation. The di erential expression, tissue localization, and functional studies demonstrate the importance of elf3 in modulating interactions between various components of the cytoskeleton proteins controlling liver and bile duct development.

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Section: Discussionmentioning

confidence: 97%

Section: Elf3 Maps To Mouse Chromosome 11mentioning

confidence: 99%

Section: Plasma Membranes Of Polarized Cells and Spectrins As A Membrmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Elf3 encodes a novel 200-kD β-spectrin: role in liver development

et al. 1999

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“…The membrane-associated cytoskeleton is a twodimensional network located on the cytoplasmic surface of the plasma membrane [21][22][23][24][25][26][27][28][29]. It consists mainly of flexible rod-shaped tetramers of spectrin that are joined by actin protofilaments to form five-or sixsided polygons.…”

Section: Introductionmentioning

confidence: 99%

Spectrin's E2/E3 ubiquitin conjugating/ligating activity is diminished in sickle cells

2005

Self Cite

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Erythrocyte spectrin contains E2/E3 ubiquitin conjugating/ligating activity in its a subunit. Ankyrin is a target of spectrin's E2/E3 ubiquitin conjugating/ligating activity in vitro and in vivo. We compare the ubiquitination levels of ankyrin mediated by control and sickle cell spectrin using a biotinylated ubiquitin cell-free assay. Sickle cell spectrin has diminished ability to transfer ubiquitin from an intermediate spectrin-ubiquitin thioester adduct (a 0 spectrin) to ankyrin, which may be due to glutathiolation of spectrin's E2 and/ or E3 active site cysteines. There is also a diminished ability of the sickle cell ankyrin to serve as target of spectrin's E2/E3 activity, probably due to oxidative damage to ankyrin. A direct correlation exists between the a 0 /a spectrin ratio and spectrin's ability to ubiquitinate ankyrin. There is also an inverse correlation between severity of the disease and the a 0 /a spectrin ratio in SS erythrocytes. These results suggest that reduced spectrin E2/ E3 activity is an important determinant of sickle cell severity. Am. J. Hematol. 79:89-96, 2005.

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Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton

Morrow

Rimm

Kennedy

et al. 1997

Comprehensive Physiology

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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 Protein 4.1 Adducin Dematin (Protein 4.9) Pallidin (Protein 4.2) p55 (an Erythrocyte Membrane‐Associated Guanylate Kinase) Stomatin Tropomyosin and Tropomodulin Dynamin Interactions with Phospholipids The Spectrin Skeleton of Non‐Erythroid Cells Spatial and Temporal Polarization Proteins Interacting with Spectrin in Non‐Erythroid Cells Cytoskeletal Elements Adhesion Proteins Evolving Concepts Conclusions: The Linked Mosaic Model

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Brain spectrin: Of mice and men

Cited by 122 publications

References 113 publications

Elf3 encodes a novel 200-kD β-spectrin: role in liver development

Elf3 encodes a novel 200-kD β-spectrin: role in liver development

Spectrin's E2/E3 ubiquitin conjugating/ligating activity is diminished in sickle cells

Of Membrane Stability and Mosaics: The Spectrin Cytoskeleton

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