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

M Kriajevska, I B Bronstein, D J Scott, S Tarabykina, M Fischer-Larsen, O Issinger, E Lukanidin

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 2000-Dec-20
OriginalsprogEngelsk
TidsskriftBBA General Subjects
Vol/bind1498
Udgave nummer2-3
Sider (fra-til)252-63
Antal sider11
ISSN0304-4165
DOI
StatusUdgivet - 20. dec. 2000

Fingeraftryk

Myosin Heavy Chains
Casein Kinase II
EF Hand Motifs
Egtazic Acid
S100 Calcium-Binding Protein A4
Enzymes

Citer dette

Kriajevska, M ; Bronstein, I B ; Scott, D J ; Tarabykina, S ; Fischer-Larsen, M ; Issinger, O ; Lukanidin, E. / Metastasis-associated protein Mts1 (S100A4) inhibits CK2-mediated phosphorylation and self-assembly of the heavy chain of nonmuscle myosin. I: BBA General Subjects. 2000 ; Bind 1498, Nr. 2-3. s. 252-63.
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title = "Metastasis-associated protein Mts1 (S100A4) inhibits CK2-mediated phosphorylation and self-assembly of the heavy chain of nonmuscle myosin.",
abstract = "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.",
keywords = "Blood Platelets, Casein Kinase II, Cells, Cultured, Enzyme Activation, Humans, Myosin Heavy Chains, Peptide Mapping, Phosphorylation, Protein-Serine-Threonine Kinases, S100 Proteins, Solubility, Trypsin",
author = "M Kriajevska and Bronstein, {I B} and Scott, {D J} and S Tarabykina and M Fischer-Larsen and O Issinger and E Lukanidin",
year = "2000",
month = "12",
day = "20",
doi = "10.1016/S0167-4889(00)00100-2",
language = "English",
volume = "1498",
pages = "252--63",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "2-3",

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Metastasis-associated protein Mts1 (S100A4) inhibits CK2-mediated phosphorylation and self-assembly of the heavy chain of nonmuscle myosin. / Kriajevska, M; Bronstein, I B; Scott, D J; Tarabykina, S; Fischer-Larsen, M; Issinger, O; Lukanidin, E.

I: BBA General Subjects, Bind 1498, Nr. 2-3, 20.12.2000, s. 252-63.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Metastasis-associated protein Mts1 (S100A4) inhibits CK2-mediated phosphorylation and self-assembly of the heavy chain of nonmuscle myosin.

AU - Kriajevska, M

AU - Bronstein, I B

AU - Scott, D J

AU - Tarabykina, S

AU - Fischer-Larsen, M

AU - Issinger, O

AU - Lukanidin, E

PY - 2000/12/20

Y1 - 2000/12/20

N2 - 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.

AB - 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.

KW - Blood Platelets

KW - Casein Kinase II

KW - Cells, Cultured

KW - Enzyme Activation

KW - Humans

KW - Myosin Heavy Chains

KW - Peptide Mapping

KW - Phosphorylation

KW - Protein-Serine-Threonine Kinases

KW - S100 Proteins

KW - Solubility

KW - Trypsin

U2 - 10.1016/S0167-4889(00)00100-2

DO - 10.1016/S0167-4889(00)00100-2

M3 - Journal article

C2 - 11108967

VL - 1498

SP - 252

EP - 263

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 2-3

ER -