PMID:16546177

Citation	Goldberg, JM, Wolpin, ES, Bosgraaf, L, Clarkson, BK, Van Haastert, PJ and Smith, JL (2006) Myosin light chain kinase A is activated by cGMP-dependent and cGMP-independent pathways. FEBS Lett. 580:2059-64
Abstract	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.
Links	PubMed Online version:10.1016/j.febslet.2006.03.008
Keywords	Animals; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Chemotaxis; Concanavalin A/pharmacology; Cyclic GMP/metabolism; Cyclic GMP/pharmacology; Cytokinesis; Dictyostelium/cytology; Dictyostelium/drug effects; Dictyostelium/enzymology; Enzyme Activation/drug effects; Gene Deletion; Intracellular Signaling Peptides and Proteins/chemistry; Intracellular Signaling Peptides and Proteins/metabolism; Models, Biological; Myosin Light Chains/metabolism; Myosin-Light-Chain Kinase/metabolism; Phosphorylation; Signal Transduction/drug effects
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