A protein immunologically related to erythrocyte band 4.1 is found on stress fibres of non-erythroid cells View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1982-10

AUTHORS

Carl M. Cohen, Susan F. Foley, Catherine Korsgren

ABSTRACT

Erythrocyte band 4.1 is one of the three major structural proteins of the erythrocyte cytoskeleton, along with spectrin and actin1–3. When bound to the tail-end of the actin-binding protein spectrin, band 4.1 is capable of promoting the formation of stable ternary complexes with spectrin and F-actin4–7, both in solution and on the erythrocyte membrane8. Recent work has demonstrated that proteins immunologically and structurally related to spectrin, as well as ankyrin—spectrin's membrane attachment site—are present in a wide variety of non-erythroid cells9–13, although the function of these proteins in such cells is still unclear. It has been reported14 that band 4.1 is present in platelets and granulocytes. Here we show that a protein immunologically related to band 4.1 is present in a non-erythroid cell, the fibroblast, and appears by immunofluorescent labelling to be distributed uniformly along stress fibres. We suggest that by analogy with erythrocyte band 4.1 this protein may be an accessory actin-binding protein, and may serve to integrate actin filaments and actin-binding proteins. More... »

PAGES

648

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/299648a0

DOI

http://dx.doi.org/10.1038/299648a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1006256775

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/6750415


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