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A caldesmon peptide activates smooth muscle via a mechanism similar to ERK‐mediated phosphorylation
Author(s) -
Huang Renjian,
Wang C.-L. Albert
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.11.047
Subject(s) - caldesmon , phosphorylation , actin , microbiology and biotechnology , peptide , biophysics , chemistry , extracellular , contraction (grammar) , biochemistry , biology , calmodulin , endocrinology , enzyme
Caldesmon (CaD) is thought to regulate smooth muscle contraction, because it binds actin and inhibits actomyosin interactions. A synthetic actin‐binding peptide (GS17C) corresponding to Gly666–Ser682 of chicken gizzard CaD has been shown to induce force development in permeabilized smooth muscle cells. The mechanism of GS17C's action remains unclear, although a structural effect was postulated. By photo‐crosslinking and fluorescence quenching experiments with a gizzard CaD fragment (H32K; Met563‐Pro771) and its mutants, we showed that GS17C indeed dissociated the C‐terminal region of H32K from actin, in a manner similar to extracellular signal‐regulated kinase‐mediated phosphorylation, thereby reversing the CaD‐imposed inhibition and enabling the actomyosin interaction.