Forskning ved Københavns Universitet - Københavns Universitet

Forside

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

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • Marina Kriajevska
  • Svetlana Tarabykina
  • Igor Bronstein
  • Norman Maitland
  • Mikhail Lomonosov
  • Hansen, Klaus
  • Georgii Georgiev
  • Eugene Lukanidin

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.

OriginalsprogEngelsk
TidsskriftJournal of Biological Chemistry
Vol/bind273
Udgave nummer16
Sider (fra-til)9852-9856
Antal sider5
ISSN0021-9258
DOI
StatusUdgivet - 17 apr. 1998
Eksternt udgivetJa

ID: 218255580