Association of v-Mos with soluble vimentin in vitro and in transformed cells.
Our previous studies have shown that vimentin can serve as a substrate for the v-Mos protein kinase in vitro. Furthermore, the amount of vimentin molecules in Moloney murine sarcoma virus (Mo-MuSV) transformed cells is decreased relative to uninfected cells and a lower molecular weight form is observed in these v-mos transformed cells (Singh & Arlinghaus, Virology 173: 144-156, 1989). Vimentin filaments are hyperphosphorylated and disassemble when cells enter mitosis. Here, we show that vimentin was coprecipitated with p85gag-mos from mitotic cell extracts by two different anti-Mos antibodies that do not crossreact with vimentin. However, we were unable to detect vimentin/v-Mos complexes interphase extracts, possibly due to lack of soluble vimentin. p37env-mos was also found to associate with purified bovine lens vimentin in vitro. The significance of these findings with regard to v-mos-induced cellular transformation is discussed.
Bai
W
W
Department of Molecular Pathology, University of Texas M.D. Anderson Cancer Center, Houston 77030.
Arlinghaus
R B
RB
Singh
B
B
D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002471:Cell Transformation, Neoplastic / Q000378:metabolism*; D003429:Cross Reactions; D051379:Mice; D008938:Mitosis; D008969:Molecular Sequence Data; D017232:Oncogene Proteins v-mos / Q000276:immunology / Q000378:metabolism*; D011233:Precipitin Tests; D011817:Rabbits; D051381:Rats; D014746:Vimentin / Q000276:immunology / Q000378:metabolism*
D017232:Oncogene Proteins v-mos; D014746:Vimentin