Antibody-induced linkages of plasma membrane proteins to intracellular actomyosin-containing filaments in cultured fibroblasts - PubMed
Antibody-induced linkages of plasma membrane proteins to intracellular actomyosin-containing filaments in cultured fibroblasts
J F Ash et al. Proc Natl Acad Sci U S A. 1977 Dec.
Abstract
The surface distributions of three different membrane integral proteins, beta2-microglobulin (part of the histocompatibility antigen complex), aminopeptidase (alpha-aminoacyl-peptide hydrolase; EC 3.4.11.2), and the Na+,K+-ATPase (ATP phosphohydrolase; EC 3.6.1.3) on human fibroblasts grown in monolayer culture have been studied with their specific antibodies by immunofluorescence. On the same cells, the distribution of intracellular actin was observed by a spectrally distinct fluorescent staining procedure. If each of the antibody reagents was permitted to cluster its specific protein in the plane of the membrane, these clusters apparently became linked, through the membrane, to actin- and myosin-containing filaments (stress fibers) underneath the membrane, and were thereby immobilized. From these and other experiments, it appears that most, if not all, integral proteins can, upon clustering, form such transmembrane linkages to actin and myosin. A molecular mechanism for the formation of these linkages is proposed which postulates that actin is associated with the cytoplasmic surface of plasma membranes by peripheral attachment to a ubiquitous integral protein X in the membrane; when other integral proteins are induced to form clusters, they become bound to X and hence to actin (and myosin). The possible physiological role of these transmembrane linkages is briefly discussed.
Similar articles
-
Transmembrane interactions and the mechanisms of transport of proteins across membranes.
Singer SJ, Ash JF, Bourguignon LY, Heggeness MH, Louvard D. Singer SJ, et al. J Supramol Struct. 1978;9(3):373-89. doi: 10.1002/jss.400090308. J Supramol Struct. 1978. PMID: 748682
-
A molecular pathway for myosin II recruitment to stress fibers.
Tojkander S, Gateva G, Schevzov G, Hotulainen P, Naumanen P, Martin C, Gunning PW, Lappalainen P. Tojkander S, et al. Curr Biol. 2011 Apr 12;21(7):539-50. doi: 10.1016/j.cub.2011.03.007. Epub 2011 Mar 31. Curr Biol. 2011. PMID: 21458264
-
Bourguignon LY, Singer SJ. Bourguignon LY, et al. Proc Natl Acad Sci U S A. 1977 Nov;74(11):5031-5. doi: 10.1073/pnas.74.11.5031. Proc Natl Acad Sci U S A. 1977. PMID: 337308 Free PMC article.
-
Köster DV, Husain K, Iljazi E, Bhat A, Bieling P, Mullins RD, Rao M, Mayor S. Köster DV, et al. Proc Natl Acad Sci U S A. 2016 Mar 22;113(12):E1645-54. doi: 10.1073/pnas.1514030113. Epub 2016 Feb 29. Proc Natl Acad Sci U S A. 2016. PMID: 26929326 Free PMC article.
-
Ras-related GTPases and the cytoskeleton.
Hall A. Hall A. Mol Biol Cell. 1992 May;3(5):475-9. doi: 10.1091/mbc.3.5.475. Mol Biol Cell. 1992. PMID: 1611153 Free PMC article. Review.
Cited by
-
Doyle C, Roth MG, Sambrook J, Gething MJ. Doyle C, et al. J Cell Biol. 1985 Mar;100(3):704-14. doi: 10.1083/jcb.100.3.704. J Cell Biol. 1985. PMID: 3972890 Free PMC article.
-
Structural and functional membrane polarity in cultured monolayers of MDCK cells.
Cereijido M, Ehrenfeld J, Meza I, Martínez-Palomo A. Cereijido M, et al. J Membr Biol. 1980;52(2):147-59. doi: 10.1007/BF01869120. J Membr Biol. 1980. PMID: 6245216
-
Riedel H. Riedel H. J Virol. 1985 Apr;54(1):224-8. doi: 10.1128/JVI.54.1.224-228.1985. J Virol. 1985. PMID: 2983116 Free PMC article.
-
Tooze J, Hollinshead M. Tooze J, et al. J Cell Biol. 1992 Aug;118(4):813-30. doi: 10.1083/jcb.118.4.813. J Cell Biol. 1992. PMID: 1500425 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials