| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
(Received for publication, March 12, 1996, and in revised form, August 19, 1996)
From the Department of Cardiac Medicine, Imperial College School of
Medicine at the National Heart and Lung Institute, Dovehouse Street,
London SW3 6LY, United Kingdom
We have investigated the mechanism of inhibition
of the actomyosin MgATPase by the smooth muscle protein calponin. We
have shown previously the specific interaction of calponin with
Glu334 of actin (EL-Mezgueldi, M., Fattoum, A., Derancourt,
J., and Kassab, R. (1992) J. Biol. Chem. 267,
15943-15951). This residue is within the sequence 332-334, which has
been proposed to be an important part of the strong myosin binding site
(Rayment, I., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M.,
Holmes, K. C., and Milligan, R. A. (1993) Science 261,
58-65). Therefore, we suggested that calponin will affect the strong
binding actin-myosin interaction. To test this hypothesis we have
investigated the effect of calponin on the strong binding of
S-1·MgAMP-PNP (5
Volume 271, Number 45,
Issue of November 8, 1996
pp. 28161-28167
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-adenylyl imidodiphosphate) and on the weak binding
of S-1·MgADP·Pi to actin. We found that an inhibitory
concentration of calponin decreased the binding of S-1·MgAMP-PNP to
actin but had no effect on the binding of S-1·MgADP·Pi.
Similar results were obtained with skeletal muscle and smooth muscle
S-1. In competition experiments calponin was found to displace
S-1·MgAMP-PNP and S-1·MgADP but not S-1·MgADP·Pi
from the actin filament. S-1 displaced calponin from actin in the rigor
state, in the presence of MgADP, and in the presence of MgAMP-PNP. We
conclude that calponin inhibits the actin activated S-1 ATPase by
blocking a strong S-1 binding site on actin and does not block the weak
binding site.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  N. Takizawa, R. Ikebe, M. Ikebe, and E. J. Luna Supervillin slows cell spreading by facilitating myosin II activation at the cell periphery J. Cell Sci., November 1, 2007; 120(21): 3792 - 3803. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. J. Babu, G. Celia, A. Y. Rhee, H. Yamamura, K. Takahashi, F. V. Brozovich, G. Osol, and M. Periasamy Effects of h1-calponin ablation on the contractile properties of bladder versus vascular smooth muscle in mice lacking SM-B myosin J. Physiol., December 15, 2006; 577(3): 1033 - 1042. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. V. Razumova, J. F. Shaffer, A.-Y. Tu, G. V. Flint, M. Regnier, and S. P. Harris Effects of the N-terminal Domains of Myosin Binding Protein-C in an in Vitro Motility Assay: EVIDENCE FOR LONG-LIVED CROSS-BRIDGES J. Biol. Chem., November 24, 2006; 281(47): 35846 - 35854. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Burgstaller, W. J. Kranewitter, and M. Gimona The molecular basis for the autoregulation of calponin by isoform-specific C-terminal tail sequences J. Cell Sci., May 15, 2002; 115(10): 2021 - 2029. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Yamamura, M. Hashio, M. Noguchi, Y. Sugenoya, M. Osakada, N. Hirano, Y. Sasaki, T. Yoden, N. Awata, N. Araki, et al. Identification of the Transcriptional Regulatory Sequences of Human Calponin Promoter and Their Use in Targeting a Conditionally Replicating Herpes Vector to Malignant Human Soft Tissue and Bone Tumors Cancer Res., May 1, 2001; 61(10): 3969 - 3977. [Abstract] [Full Text]
|
|
|
|
|
|
M Gimona and R Mital The single CH domain of calponin is neither sufficient nor necessary for F-actin binding J. Cell Sci., January 7, 1998; 111(13): 1813 - 1821. [Abstract] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
