By the same authors

From the same journal

From the same journal

Metastasis-associated Mts1 (S100A4) protein modulates protein kinase C phosphorylation of the heavy chain of nonmuscle myosin

Research output: Contribution to journalArticle

Standard

Metastasis-associated Mts1 (S100A4) protein modulates protein kinase C phosphorylation of the heavy chain of nonmuscle myosin. / Kriajevska, M; Tarabykina, S; Bronstein, I; Maitland, N; Lomonosov, M; Hansen, K; Georgiev, G; Lukanidin, E.

In: Journal of Biological Chemistry, Vol. 273, No. 16, 17.04.1998, p. 9852-9856.

Research output: Contribution to journalArticle

Harvard

Kriajevska, M, Tarabykina, S, Bronstein, I, Maitland, N, Lomonosov, M, Hansen, K, Georgiev, G & Lukanidin, E 1998, 'Metastasis-associated Mts1 (S100A4) protein modulates protein kinase C phosphorylation of the heavy chain of nonmuscle myosin', Journal of Biological Chemistry, vol. 273, no. 16, pp. 9852-9856.

APA

Kriajevska, M., Tarabykina, S., Bronstein, I., Maitland, N., Lomonosov, M., Hansen, K., ... Lukanidin, E. (1998). Metastasis-associated Mts1 (S100A4) protein modulates protein kinase C phosphorylation of the heavy chain of nonmuscle myosin. Journal of Biological Chemistry, 273(16), 9852-9856.

Vancouver

Kriajevska M, Tarabykina S, Bronstein I, Maitland N, Lomonosov M, Hansen K et al. Metastasis-associated Mts1 (S100A4) protein modulates protein kinase C phosphorylation of the heavy chain of nonmuscle myosin. Journal of Biological Chemistry. 1998 Apr 17;273(16):9852-9856.

Author

Kriajevska, M ; Tarabykina, S ; Bronstein, I ; Maitland, N ; Lomonosov, M ; Hansen, K ; Georgiev, G ; Lukanidin, E. / Metastasis-associated Mts1 (S100A4) protein modulates protein kinase C phosphorylation of the heavy chain of nonmuscle myosin. In: Journal of Biological Chemistry. 1998 ; Vol. 273, No. 16. pp. 9852-9856.

Bibtex - Download

@article{6af41754310347de9c981e3b87d2e5a7,
title = "Metastasis-associated Mts1 (S100A4) protein modulates protein kinase C phosphorylation of the heavy chain of nonmuscle myosin",
abstract = "Mts1 protein (S100A4 according to a new classification) has been implicated in the formation of the metastatic phenotype via regulation of cell motility and invasiveness, Previously we have demonstrated that Mts1 protein interacted with the heavy chain of nonmuscle myosin in a calcium-dependent manner. To elucidate the role of the Mts1-myosin interaction, we mapped the Mts1-binding region on the myosin heavy chain molecule. We prepared proteolytically digested platelet myosin and a series of overlapped myosin heavy chain protein fragments and used them in a blot overlay with Mts1 protein. Here we report that the Mts1-binding site is located within a 29-amino acid region, at the C-terminal end of the myosin heavy chain (between 1909-1937 amino acids). Two-dimensional phosphopeptide analysis showed that Mts1 protein inhibits protein kinase C phosphorylation of the platelet myosin heavy chain at Ser-1917. We hypothesize that Mts1 protein regulates cytoskeletal dynamics of the metastatic cells through modulation of the myosin phosphorylation by protein kinase C in calcium-dependent fashion.",
keywords = "CALCIUM-BINDING PROTEIN, CELL-LINE, MAMMARY ADENOCARCINOMA, MESSENGER-RNAS, PEL98 PROTEIN, GENE, EXPRESSION, CALMODULIN, IDENTIFICATION, FAMILY",
author = "M Kriajevska and S Tarabykina and I Bronstein and N Maitland and M Lomonosov and K Hansen and G Georgiev and E Lukanidin",
year = "1998",
month = "4",
day = "17",
language = "English",
volume = "273",
pages = "9852--9856",
journal = "The Journal of biological chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "16",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Metastasis-associated Mts1 (S100A4) protein modulates protein kinase C phosphorylation of the heavy chain of nonmuscle myosin

AU - Kriajevska, M

AU - Tarabykina, S

AU - Bronstein, I

AU - Maitland, N

AU - Lomonosov, M

AU - Hansen, K

AU - Georgiev, G

AU - Lukanidin, E

PY - 1998/4/17

Y1 - 1998/4/17

N2 - Mts1 protein (S100A4 according to a new classification) has been implicated in the formation of the metastatic phenotype via regulation of cell motility and invasiveness, Previously we have demonstrated that Mts1 protein interacted with the heavy chain of nonmuscle myosin in a calcium-dependent manner. To elucidate the role of the Mts1-myosin interaction, we mapped the Mts1-binding region on the myosin heavy chain molecule. We prepared proteolytically digested platelet myosin and a series of overlapped myosin heavy chain protein fragments and used them in a blot overlay with Mts1 protein. Here we report that the Mts1-binding site is located within a 29-amino acid region, at the C-terminal end of the myosin heavy chain (between 1909-1937 amino acids). Two-dimensional phosphopeptide analysis showed that Mts1 protein inhibits protein kinase C phosphorylation of the platelet myosin heavy chain at Ser-1917. We hypothesize that Mts1 protein regulates cytoskeletal dynamics of the metastatic cells through modulation of the myosin phosphorylation by protein kinase C in calcium-dependent fashion.

AB - Mts1 protein (S100A4 according to a new classification) has been implicated in the formation of the metastatic phenotype via regulation of cell motility and invasiveness, Previously we have demonstrated that Mts1 protein interacted with the heavy chain of nonmuscle myosin in a calcium-dependent manner. To elucidate the role of the Mts1-myosin interaction, we mapped the Mts1-binding region on the myosin heavy chain molecule. We prepared proteolytically digested platelet myosin and a series of overlapped myosin heavy chain protein fragments and used them in a blot overlay with Mts1 protein. Here we report that the Mts1-binding site is located within a 29-amino acid region, at the C-terminal end of the myosin heavy chain (between 1909-1937 amino acids). Two-dimensional phosphopeptide analysis showed that Mts1 protein inhibits protein kinase C phosphorylation of the platelet myosin heavy chain at Ser-1917. We hypothesize that Mts1 protein regulates cytoskeletal dynamics of the metastatic cells through modulation of the myosin phosphorylation by protein kinase C in calcium-dependent fashion.

KW - CALCIUM-BINDING PROTEIN

KW - CELL-LINE

KW - MAMMARY ADENOCARCINOMA

KW - MESSENGER-RNAS

KW - PEL98 PROTEIN

KW - GENE

KW - EXPRESSION

KW - CALMODULIN

KW - IDENTIFICATION

KW - FAMILY

M3 - Article

VL - 273

SP - 9852

EP - 9856

JO - The Journal of biological chemistry

JF - The Journal of biological chemistry

SN - 0021-9258

IS - 16

ER -