Journal
FEBS LETTERS
Volume 557, Issue 1-3, Pages 121-124Publisher
WILEY
DOI: 10.1016/S0014-5793(03)01456-X
Keywords
myosin light chain kinase; calmodulin; calcium; phosphorylation; fluorescence resonance energy transfer
Funding
- NHLBI NIH HHS [HL29043] Funding Source: Medline
- NIDDK NIH HHS [DK53863] Funding Source: Medline
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Myosin II regulatory light chain (RLC) phosphorylation by Ca2+/calmodulin (CaM)-dependent myosin light chain kinase (MLCK) is implicated in many cellular actin cytoskeletal functions. We examined MLCK activation quantitatively with a fluorescent biosensor MLCK where Ca2+-dependent increases in kinase activity were coincident with decreases in fluorescence resonance energy transfer (FRET) in vitro. In cells stably transfected with CaM sensor MLCK, increasing [Ca2+](i) increased MLCK activation and RLC phosphorylation coincidently. There was no evidence for CaM binding but not activating MLCK at low [Ca2+](i). At saturating [Ca2+](i), MLCK was not fully activated probably due to limited availability of cellular Ca2+/CaM. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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