cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human a-fodrin

McMahon, Andrew P.; Giebelhaus, Dawn H.; Champion, Janet; Bailes, Juliet A.; Lacey, Simon F.; Carritt, B.; Henchman, Susan K.; Moon, Randall T.

doi:10.1111/j.1432-0436.1987.tb00072.x

Cited by 14 publications

(27 citation statements)

References 20 publications

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“…Comparison of the present sequence with the published spectrin sequences corroborated the early observation (see McMahon et al, 1987 for detailed analysis) that the nonerythroid c~-spectrins from different species, ranging in this study from Xenopus to man, show a high degree of mutual homology while the mammalian erythroid a-spectrin is a more distant protein. This indicates a rapid divergent evolution of the latter.…”

Section: Comparison Of Various Spectrinssupporting

confidence: 88%

“…It also confirms that the 60-bp insert found in one of the clones of McMahon et al (1987) represents the predominant transcript and is not a cloning artifact since the same sequence is present here (amino acid residues 1,053-1,073). The observation of McMahon et al (1987) that there is a 36 amino acid extension in call (residues 1,168-1,204 in our sequence) is also corroborated by our sequence.…”

Section: Comparison Of Various A-spectrinssupporting

confidence: 81%

“…This finding was confirmed by Birkenmeier et al (1985). Later, McMahon et al (1987), Leto et al (1988), and Giebelhaus et al (1987) have provided…”

mentioning

confidence: 61%

“…The Eco RI site in CLONE I was not overlapped by sequencing. However, a previously determined homologous sequence has already covered this site (McMahon et al, 1987).…”

Section: The Nucleotide and Deduced Amino Acid Sequence Of The Brain mentioning

confidence: 99%

“…5. The published Xenopus oocyte ~-speetrin sequence corresponds to the residues 568-1,021, the human fibroblast ct-spectrin sequence (McMahon et al, 1987) to the residues 676-1,599, and the rat brain c~-spectrin sequence (Leto et al, 1988) to the residues 1,776-2,250. The fragments of the human erythroid t~-spectrin sequence (Speicher and Marchesi, 1984) cover scattered parts along the chicken sequence except the COOH terminus.…”

Section: Comparison Of Various A-spectrinsmentioning

confidence: 99%

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Primary structure of the brain alpha-spectrin [published erratum appears in J Cell Biol 1989 Mar;108(3):following 1175]

Wasenius

1989

The Journal of Cell Biology

157

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Abstract. We have determined the nucleotide sequence coding for the chicken brain a-spectrin. It is derived both from the cDNA and genomic sequences, comprises the entire coding frame, 5' and 3' untranslated sequences, and terminates in the poly(A)-tail. The deduced amino acid sequence was used to map the domain structure of the protein. The a-chain of brain spectrin contains 22 segments of which 20 correspond to the repeat of the human erythrocyte spectrin (Speicher, D. W., and V. T. Marchesi. 1984. Nature (Lond.). 311:177-180.), typically made of 106 residues. These homologous segments probably account for the flexible, rod-like structure of spectrin. Secondary structure prediction suggests predominantly a-helical structure for the entire chain.Parts of the primary structure are excluded from the repetitive pattern and they reside in the middle part of the sequence and in its COOH terminus. Search for homology in other proteins showed the presence of the following distinct structures in these nonrepetitive regions: (a) the COOH-terminal part of the molecule that shows homology with a-actinin, (b) two typical EF-hand (i.e., Ca:*-binding) structures in this region, (c) a sequence close to the EF-hand that fulfills the criteria for a calmodulin-binding site, and (d) a domain in the middle of the sequence that is homologous to a NH2-terminal segment of several src-tyrosine kinases and to a domain of phospholipase C. These regions are good candidates to carry some established as well as some yet unestablished functions of spectrin. Comparative analysis showed that a-spectrin is well conserved across the species boundaries from Xenopus to man, and that the human erythrocyte a-spectrin is divergent from the other spectrins.

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Section: Comparison Of Various Spectrinssupporting

confidence: 88%

Section: Comparison Of Various A-spectrinssupporting

confidence: 81%

“…This finding was confirmed by Birkenmeier et al (1985). Later, McMahon et al (1987), Leto et al (1988), and Giebelhaus et al (1987) have provided…”

mentioning

confidence: 61%

“…The Eco RI site in CLONE I was not overlapped by sequencing. However, a previously determined homologous sequence has already covered this site (McMahon et al, 1987).…”

Section: The Nucleotide and Deduced Amino Acid Sequence Of The Brain mentioning

confidence: 99%

Section: Comparison Of Various A-spectrinsmentioning

confidence: 99%

See 3 more Smart Citations

Primary structure of the brain alpha-spectrin [published erratum appears in J Cell Biol 1989 Mar;108(3):following 1175]

Wasenius

1989

The Journal of Cell Biology

157

View full text Add to dashboard Cite

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Two populations of β-spectrin in rat skeletal muscle

Porter¹,

Scher²,

Resneck³

et al. 1997

Cell Motil. Cytoskeleton

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Composition and expression of spectrin‐based membrane skeletons in non‐erythroid cells

Moon¹,

McMahon

1987

BioEssays

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Cellular differentiation is often accompanied by the expression of specialized plasma membrane proteins which accumulate in discrete regions. The biogenesis of these specialized membrane domains involves the assembly and co‐localisation of a spectrin‐based membrane skeleton. While the constituents of the membrane skeleton in non‐erythroid cells are often immunologically related to erythroid spectrin, ankyrin, and protein 4.1, there are structural and functional differences between the isoforms of these membrane skeleton polypeptides, as well as highly variable patterns of expression during cellular differentiation. We consider this heterogeneity of structure and expression during development in the context of the hypothesis that non‐erythroid spectrin, ankyrin, and protein 4.1 are involved in the formation of specialized membrane domains.

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cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human a-fodrin

Abstract: Differentiation (1987) 34: 68-78 The legend to Fig. 7a, b contained three printing errors (p instead of 4). The correct reading of lanes 1-5 is as follows: Lane 1, lpter-lp34; lane 2, lp34-lqter; lane 3, lp34-lqter; lane 4 , lpter-lp36.13; lane 5, lp36.13-lqter;

Cited by 14 publications

References 20 publications

Primary structure of the brain alpha-spectrin [published erratum appears in J Cell Biol 1989 Mar;108(3):following 1175]

Primary structure of the brain alpha-spectrin [published erratum appears in J Cell Biol 1989 Mar;108(3):following 1175]

Two populations of β-spectrin in rat skeletal muscle

Composition and expression of spectrin‐based membrane skeletons in non‐erythroid cells

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