pp39mos is associated with p34cdc2 kinase in c-mosxe-transformed NIH 3T3 cells

Renping Zhou, Ira Daar, Douglas K. Ferris, Gretchen White, Richard S. Paules, George Vande Woude

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

We investigated the possible interactions between pp39mos and p34cdc2 kinase in NIH 3T3 cells transformed by c-mosxe · pp39mos is coprecipitated with p34cdc2 when using either anti-PSTAIR antibody or p13suc1-Sepharose beads. Likewise, p34cdc2 is coprecipitated with pp39mos when using anti-mos antibody. However, pp39mos was not present in histone H1 kinase-active p34cdc2 complexes precipitated with anti-p34cdc2 C-terminal peptide antibody even during metaphase of the cell cycle. The molar ratio of p34 to pp39mos in the p13suc1 complex is ∼2:1. Consistent with the tight association between pp39mos and tubulin, tubulin was also present in equivalent amounts with pp39mos and p34 in the p13suc1 complex. This pp39mos-p34cdc2-tubulin complex may be important in transformation by the mos oncogene.

Original languageEnglish (US)
Pages (from-to)3583-3589
Number of pages7
JournalMolecular and cellular biology
Volume12
Issue number8
StatePublished - Aug 1992
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'pp39mos is associated with p34cdc2 kinase in c-mosxe-transformed NIH 3T3 cells'. Together they form a unique fingerprint.

Cite this