Tropomodulin binds to filensin intermediate filaments

被引:19
作者
Fischer, RS [1 ]
Quinlan, RA
Fowler, VM
机构
[1] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA
[2] Univ Durham, Sch Biol & Biomed Sci, Durham DH1 3LE, England
关键词
actin; intermediate filament; lens; cytoskeleton; tropomodulin;
D O I
10.1016/S0014-5793(03)00711-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Tropomodulin (Tmod) is an actin filament pointed end capping protein found in the membrane skeleton of lens fiber cells. We demonstrate that Tmod4 is able to bind the lens-specific intermediate filament protein, filensin, in either co-sedimentation or solid phase binding assays in a saturable fashion, but with low affinity and stoichiometry. Furthermore, Tmod4 does not bind the 53 kDa rod domain of filensin, nor to CP49, the obligate assembly partner of filensin. Finally, the binding of filensin to Tmod4 does not inhibit the actin capping activity of Tmod4 in vitro, suggesting that the two functions are not mutually exclusive. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:228 / 232
页数:5
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