Title : Characterization of Ca2+/calmodulin-dependent protein kinase I as a myosin II regulatory light chain kinase in vitro and in vivo.

Pub. Date : 2002 Oct 15

PMID : 12081505






2 Functional Relationships(s)
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1 In this report, we demonstrate that CaM-KI activated by an upstream kinase (CaM-K kinase), but not unactivated CaM-KI, phosphorylates myosin II regulatory light chain (MRLC) efficiently ( K (cat), 1.7 s(-1)) and stoichiometrically (approximately 0.8 mol of phosphate/mol) in a Ca(2+)/CaM-dependent manner in vitro. cafestol palmitate myosin heavy chain 14 Homo sapiens
2 Transient expression of the Ca(2+)/CaM-independent form of CaM-KI (CaM-KI(1-293)) in HeLa cells induced Ser-19 phosphorylation of myosin, II accompanied by reorganization of actin filaments in the peripheral region of the cells. cafestol palmitate myosin heavy chain 14 Homo sapiens