Direct interaction of β-dystroglycan with F-actin
نویسندگان
چکیده
منابع مشابه
Direct interaction of actin filaments with F-BAR protein pacsin2.
Two mechanisms have emerged as major regulators of membrane shape: BAR domain-containing proteins, which induce invaginations and protrusions, and nuclear promoting factors, which cause generation of branched actin filaments that exert mechanical forces on membranes. While a large body of information exists on interactions of BAR proteins with membranes and regulatory proteins of the cytoskelet...
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Filamin is a major high-molecular-weight protein in smooth muscle which was recently identified and isolated [Wang, K., Ash, J. F. & Singer, S. J. (1975) Proc. Natl. Acad. Sci. U.S.A. 72, 4483-4486]. In the present studies, we shown that highly purified chicken gizzard filamin and muscle F-actin react in solution to form aggregates containing both proteins. Occasionally, these aggregates coagul...
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Attractions between like-charged polyelectrolytes have been observed in a variety of systems (W.M. Gelbart, R.F. Bruinsma, P.A. Pincus, V.A. Parsegian, Phys. Today 53, September issue, 38 (2000)). Recent biological examples include DNA, filamentous viruses, and F-actin. Theoretical investigations on idealized systems indicate that counterion correlations play a central role, but no experiments ...
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15 صفحه اولDirect interaction of the trans-Golgi network membrane protein, TGN38, with the F-actin binding protein, neurabin.
TGN38 is a type I integral membrane protein that constitutively cycles between the trans-Golgi network (TGN) and plasma membrane. The cytosolic domain of TGN38 interacts with AP2 clathrin adaptor complexes via the tyrosine-containing motif (-SDYQRL-) to direct internalization from the plasma membrane. This motif has previously been shown to direct both internalization and subsequent TGN targeti...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2003
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20030808