Influence of the effector peptide of MARCKS-related protein on actin polymerization: a kinetic analysis

Citation
F. Wohnsland et al., Influence of the effector peptide of MARCKS-related protein on actin polymerization: a kinetic analysis, BIOPHYS CH, 85(2-3), 2000, pp. 169-177
Citations number
37
Categorie Soggetti
Biochemistry & Biophysics","Physical Chemistry/Chemical Physics
Journal title
BIOPHYSICAL CHEMISTRY
ISSN journal
03014622 → ACNP
Volume
85
Issue
2-3
Year of publication
2000
Pages
169 - 177
Database
ISI
SICI code
0301-4622(20000715)85:2-3<169:IOTEPO>2.0.ZU;2-4
Abstract
The members of the MARCKS protein family, MARCKS (an acronym for myristoyla ted alanine-rich C kinase substrate) and MARCKS-related protein (MRP), inte ract with membranes, protein kinase C, and calmodulin via their effector do main, a highly basic segment composed of 24-25 amino acid residues. This do main is also involved in the interaction between MARCKS/MRP and actin. In t his article we show that a peptide corresponding to the effector domain of MRP, the effector peptide, strongly influences the dynamics of actin polyme rization. Depending on the stoichiometric ratio of effector peptide to acti n the peptide either accelerates or retards the actin polymerization proces s, which takes place in the presence of near-physiological salt concentrati ons. A model is developed in which this phenomenon is explained by two inde pendent nucleation processes involving free actin monomers and peptide-boun d actin monomers, respectively. As a control, a possible regulatory mechani sm has been investigated: we show that calmodulin inhibits the actin polyme rizing activity of the MRP effector peptide, thereby validating our model a pproach. (C) 2000 Elsevier Science B.V. All rights reserved.