Identification of nuclear beta II protein kinase C as a mitotic lamin kinase.
作者： C A Stratton , L J Thompson , D J Burns , A P Fields , V L Goss
DOI: 10.1016/S0021-9258(17)32276-7
关键词: Kinase 、 CDC2 Protein Kinase 、 Cell cycle 、 Biology 、 Protein kinase C 、 Cyclin-dependent kinase 2 、 Lamin 、 Cyclin B 、 Molecular biology 、 Cyclin-dependent kinase complex
摘要: Multisite phosphorylation of the nuclear lamins is thought to regulate process mitotic envelope breakdown in vivo. Here we investigate involvement two proposed human lamin kinases, beta II protein kinase C (PKC) and p34cdc2/cyclin B kinase, B1 vitro intact cells. We find that both kinases can phosphorylate purified soluble at similar rates. However, PKC phosphorylates interphase more than 200 times rate kinase. PKC-mediated confined sites, Ser395 Ser405, within carboxyl-terminal domain, whereas a single site, Ser23, amino-terminal domain. A second potential site Ser393, not phosphorylated by invertebrate from sea star exhibits different specificity, phosphorylating amino- sites. Mitotic cells predominantly its Comparative tryptic phosphopeptide mapping demonstrates prominent target translocates nucleus during G2/M phase cell cycle concomitant with indicating physiologic role for activation The presence sites domain which are either or suggests other kinase(s) phosphorylation.
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