Metastasis-associated protein Mts1 (S100A4) inhibits CK2-mediated phosphorylation and self-assembly of the heavy chain of nonmuscle myosin

被引:51
作者
Kriajevska, M
Bronstein, IB
Scott, DJ
Tarabykina, S
Fischer-Larsen, M
Issinger, OG
Lukanidin, E
机构
[1] Danish Canc Soc, Inst Canc Biol, Dept Mol Canc Biol, DK-2100 Copenhagen, Denmark
[2] Univ York, Dept Chem, York Struct Biol Lab, York YO10 5DD, N Yorkshire, England
[3] Univ York, Dept Biol, York YO10 5DD, N Yorkshire, England
[4] Univ So Denmark, Dept Biochem & Mol Biol, DK-5230 Odense, Denmark
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2000年 / 1498卷 / 2-3期
关键词
S100A4; nonmuscle myosin; protein kinase CK2; self-assembly of myosin;
D O I
10.1016/S0167-4889(00)00100-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A role for EF-hand calcium-binding protein Mts1 (S100A4) in the phosphorylation and the assembly of myosin filaments was studied. The nonmuscle myosin molecules form bipolar filaments, which interact with actin filaments to produce a contractile force. Phosphorylation of the myosin plays a regulatory role in the myosin assembly. In the presence of calcium, Mts1 binds at the C-terminal end of the myosin heavy chain close to the site of phosphorylation by protein kinase CK2 (Ser1944). In the present study, we have shown that interaction of Mts1 with the human platelet myosin or C-terminal fragment of the myosin heavy chain inhibits phosphorylation of the myosin heavy chain by protein kinase CK2 in vitro. Mts1 might also bind directly the beta subunit of protein kinase CK2, thereby modifying the enzyme activity. Our results indicate that myosin oligomers were disassembled in the presence of Mts1. The short C-terminal fragment of the myosin heavy chain was totally soluble in the presence of an equimolar amount of Mts1 at low ionic conditions (50 mM NaCl). Depolymerization was found to be calcium-dependent and could be blocked by EGTA. Our data suggest that Mts1 can increase myosin solubility and therefore suppress its assembly. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:252 / 263
页数:12
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