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Myosin light chains are not a physiological substrate of AMPK in the control of cell structure changes
Author(s) -
Bultot Laurent,
Horman Sandrine,
Neumann Dietbert,
Walsh Michael P.,
Hue Louis,
Rider Mark H.
Publication year - 2009
Publication title -
febs letters
Language(s) - Slovak
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.11.022
Subject(s) - ampk , protein kinase a , uniprot , chemistry , myosin , myosin light chain kinase , phosphorylation , kinase , substrate (aquarium) , biochemistry , microbiology and biotechnology , biology , ecology , gene
MINT‐ 6800264 : smMLCK (uniprotkb: P11799 ) phosphorylates (MI: 0217 ) MLC (uniprotkb: P08590 ) by protein kinase assay (MI: 0424 ) MINT‐ 6800252 : AMPK (uniprotkb: Q13131 ) phosphorylates (MI: 0217 ) ACC2 (uniprotkb: 000763 ) by protein kinase assay (MI: 0424 )
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