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

delete2006-08-04
delete13
PRE
AI
I
Imen Ferjani
A
Abdellatif Fattoum
S
Sutherland K. Maciver
M
Mohamed Manaï
Y
Yves Benyamin
C
Claude Roustan *
DOI:10.1016/j.febslet.2006.07.065delete
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Abstract

Abstract

En 中文
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.
Keywords:
actin
cytoskeleton
calponin
cell signalling

Journal

FEBS Letters cover
FEBS Letters
IF:
3
Papers:
2.3W
Citations:
3.8W

Organization

No organization information available