Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains |
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Authors: | Moussavi Robabeh S Kelley Christine A Adelstein Robert S |
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Institution: | (1) Laboratory of Molecular Cardiology, National Heart, Lung, and Blood Institute, National Institutes of Health, Building10, Room 8N-202, 20892 Bethesda, MD, USA |
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Abstract: | In this article we review the various amino acids present in vertebrate nonmuscle and smooth muscle myosin that can undergo phosphorylation. The sites for phosphorylation in the 20 kD myosin light chain include serine-19 and threonine-18 which are substrates for myosin light chain kinase and serine-1 and/or-2 and threonine-9 which are substrates for protein kinase C. The sites in vertebrate smooth muscle and nonmuscle myosin heavy chains that can be phosphorylated by protein kinase C and casein kinase II are also summarized.Original data indicating that treatment of human T-lymphocytes (Jurkat cell line) with phorbol 12-myristate 13-acetate results in phosphorylation of both the 20 kD myosin light chain as well as the 200 kD myosin heavy chain is presented. We identified the amino acids phosphorylated in the human T-lymphocytes myosin light chains as serine-1 or serine-2 and in the myosin heavy chains as serine-1917 by 1-dimensional isoelectric focusing of tryptic phosphopeptides. Untreated T-lymphocytes contain phosphate in the serine-19 residue of teh myosin light chain and in a residue tentatively identified as serine-1944 in the myosin heavy chain.Abbreviations MLC
myosin light chain
- MHC
myosin heavy chain
- Tris
tris(hydroxymethyl)aminomethane
- EGTA
ethylenebis(oxyethylenenitrilo)]tetraacetic acid
- EDTA
ethylenediaminetetraacetate
- TPCK
N-tosyl-L-phenylalanine chloromethyl ketone
- PMA
phorbol 12-myristate 13-acetate |
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Keywords: | myosin phosphorylation protein kinases |
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