ArticleProceedings of the National Academy of Sciences of the United States of America1989
Erythrocyte protein 4.1 binds and regulates myosin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 55 citations in OpenAlex.
- Nonequilibrium fluctuations of mechanically stretched single red blood cells detected by optical tweezers.European biophysics journal : EBJ · 2013Article
- A member of the Plasmodium falciparum PHIST family binds to the erythrocyte cytoskeleton component band 4.1.Malaria journal · 2013Article
- Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.Journal of cell science · 2011Article
- The 10 kDa domain of human erythrocyte protein 4.1 binds the Plasmodium falciparum EBA-181 protein.Malaria journal · 2006Article
- Cardiac muscle cell cytoskeletal protein 4.1: analysis of transcripts and subcellular location--relevance to membrane integrity, microstructure, and possible role in heart failure.Mammalian genome : official journal of the International Mammalian Genome Society · 2005Article
- A nonerythroid isoform of protein 4.1R interacts with components of the contractile apparatus in skeletal myofibers.Molecular biology of the cell · 2000Article
- A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein.The Journal of cell biology · 1999Article
- Mechanical fluctuations of the membrane-skeleton are dependent on F-actin ATPase in human erythrocytes.The Journal of cell biology · 1998Article
- Structural protein 4.1 in the nucleus of human cells: dynamic rearrangements during cell division.The Journal of cell biology · 1997Article
- Role of tissue specific alternative pre-mRNA splicing in the differentiation of the erythrocyte membrane.Transactions of the American Clinical and Climatological Association · 1997Review
- Characterization of isoforms of protein 4.1 present in the nucleus.The Biochemical journal · 1991Article
- Stopped-flow measurement of cytoskeletal contraction: Dictyostelium myosin II is specifically required for contraction of amoeba cytoskeletons.The Journal of cell biology · 1991Article
- Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin was recently identified in erythrocytes and was shown to partition both with membrane and cytosolic fractions, suggesting that it may be loosely bound to membranes [Fowler, V. M., Davis, J. Q. & Bennett, V. (1985) J. Cell Biol. 100, 47-55, and Wong, A. J., Kiehart, D. P. & Pollard, T. D. (1985) J. Biol. Chem. 260, 46-49]; however, the molecular basis for this binding was unclear. The present studies employed immobilized monomeric myosin to examine the interaction of myosin with erythrocyte protein 4.1. In human erythrocytes, protein 4.1 binds to integral membrane proteins and mediates spectrin-actin assembly. Protein 4.1 binds to rabbit skeletal muscle myosin with a Kd = 140 nM and a stoichiometry consistent with 1:1 binding. Heavy meromyosin competes for protein 4.1 binding with Ki = 36-54 nM; however, the S1 fragment (the myosin head) competes less efficiently. Affinity chromatography of partial chymotryptic digests of protein 4.1 on immobilized myosin identified a 10-kDa domain of protein 4.1 as the myosin-binding site. In functional studies, protein 4.1 partially inhibited the actin-activated Mg2+-ATPase activity of rabbit skeletal muscle myosin with Ki = 51 nM. Liver cytosolic and erythrocyte myosins preactivated with myosin light-chain kinase were similarly inhibited by protein 4.1. These studies show that protein 4.1 binds, modulates, and thus may regulate myosin. This interaction might serve to generate the contractile forces involved in Mg2+-ATP-dependent shape changes in erythrocytes and may additionally serve as a model for myosin organization and regulation in non-muscle cells.
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