García-Rocha M, Avila J, Lozano J
Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Spain.
Exp Cell Res. 1997 Jan 10;230(1):1-8. doi: 10.1006/excr.1996.3364.
It has been suggested that the protein kinase C zeta (zeta PKC) isoform is involved in mitogenic signaling in Xenopus oocytes and mammalian cells. Thus, the characterization of potential regulatory molecules that bind to zeta PKC is of great interest. We report here the identification by affinity chromatography of tubulin as a zeta PKC-binding protein. Further immunofluorescence and microtubule copolymerization studies are consistent with this interaction. It is suggested that tubulin binds to zeta PKC through its pseudosubstrate domain. Furthermore, results demonstrate that treatment of cells with nocodazole, which disrupts microtubule structures, severely impairs the activity of native zeta PKC, stressing the potential functional relevance of zeta PKC binding to tubulin.
有人提出蛋白激酶Cζ（ζ-PKC）亚型参与非洲爪蟾卵母细胞和哺乳动物细胞的促有丝分裂信号传导。因此，鉴定与ζ-PKC结合的潜在调节分子极具意义。我们在此报告通过亲和层析鉴定微管蛋白为一种ζ-PKC结合蛋白。进一步的免疫荧光和微管蛋白共聚研究证实了这种相互作用。提示微管蛋白通过其假底物结构域与ζ-PKC结合。此外，结果表明用诺考达唑处理细胞会破坏微管结构，严重损害天然ζ-PKC的活性，强调了ζ-PKC与微管蛋白结合的潜在功能相关性。
