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Myosin light chain kinase A is activated by cGMP‐dependent and cGMP‐independent pathways
Author(s) -
Goldberg Jonathan M.,
Wolpin Eric S.,
Bosgraaf Leonard,
Clarkson Bryan K.,
Van Haastert Peter J.M.,
Smith Janet L.
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.2006.03.008
Subject(s) - myosin light chain kinase , chemotaxis , phosphorylation , microbiology and biotechnology , myosin , cytokinesis , concanavalin a , protein kinase a , biology , chemistry , biochemistry , receptor , cell division , cell , in vitro
Stimulation of Dictyostelium cells with the chemoattractant cAMP results in transient phosphorylation of the myosin regulatory light chain (RLC). We show that myosin light chain kinase A (MLCK‐A) is responsible for RLC phosphorylation during chemotaxis, and that MLCK‐A itself is transiently phosphorylated on threonine‐166, dramatically increasing its catalytic activity. MLCK‐A activation during chemotaxis is highly responsive to cellular cGMP levels and the cGMP‐binding protein GbpC. MLCK‐A − cells have a partial cytokinesis defect, and do not phosphorylate RLC in response to concanavalin A (conA), but cells lacking cGMP or GbpC divide normally and phosphorylate in response to conA. Thus MLCK‐A is activated by a cGMP/GbpC‐independent mechanism activated during cytokinesis or by conA, and a cGMP/GbpC‐dependent pathway during chemotaxis.