Calponin binds G-actin and F-actin with similar affinity

被引:7
|
作者
Ferjani, Imen
Fattoum, Abdellatif
Maciver, Sutherland K.
Manai, Mohamed
Benyamin, Yves
Roustan, Claude
机构
[1] Univ Montpellier 2, UMR 5539, CNRS, Lab Motil Cellulaire,Ecol Prat Hautes Etud, F-34095 Montpellier 5, France
[2] Univ Edinburgh, Sch Biomed & Clin Lab Sci, Div Biomed Sci, Coll Med, Edinburgh EH8 9XD, Midlothian, Scotland
[3] CNRS, FRE 2593, Ctr Rech Biochim Macromol, F-34293 Montpellier 5, France
[4] Fac Sci Tunis, Unite Biochim & Biol Mol, Tunis, Tunisia
关键词
actin; cytoskeleton; calponin; cell signalling;
D O I
10.1016/j.febslet.2006.07.065
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
Calponins are actin-binding proteins that are implicated in the regulation of actomyosin. Calponin binds filamentous actin (F-actin) through two distinct sites ABS1 and ABS2, with an affinity in the low micromolar range. We report that smooth muscle calponin binds monomeric actin with a similar affinity (K-d of 0.15 mu M). We show that the arrangement of binding is similar to that of F-actin by a number of criteria, most notably that the distance between Cys273 on calponin and Cys374 of actin is 29, when measured by fluorescent resonance energy transfer, the same distance as previously reported for F-actin. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
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页码:4801 / 4806
页数:6
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