酪氨酸磷酸化调节Cdc48p的细胞周期依赖性核定位。
Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p.
作者信息
Madeo F, Schlauer J, Zischka H, Mecke D, Fröhlich K U
机构信息
Physiologisch-chemisches Institut der Universität Tübingen, Germany.
出版信息
Mol Biol Cell. 1998 Jan;9(1):131-41. doi: 10.1091/mbc.9.1.131.
Abstract
Cdc48p from Saccharomyces cerevisiae and its highly conserved mammalian homologue VCP (valosin-containing protein) are ATPases with essential functions in cell division and homotypic fusion of endoplasmic reticulum vesicles. Both are mainly attached to the endoplasmic reticulum, but relocalize in a cell cycle-dependent manner: Cdc48p enters the nucleus during late G1; VCP aggregates at the centrosome during mitosis. The nuclear import signal sequence of Cdc48p was localized near the amino terminus and its function demonstrated by mutagenesis. The nuclear import is regulated by a cell cycle-dependent phosphorylation of a tyrosine residue near the carboxy terminus. Two-hybrid studies indicate that the phosphorylation results in a conformational change of the protein, exposing the nuclear import signal sequence previously masked by a stretch of acidic residues.
摘要
来自酿酒酵母的Cdc48p及其高度保守的哺乳动物同源物VCP（含缬酪肽蛋白）是ATP酶，在内质网小泡的细胞分裂和同型融合中具有重要功能。两者都主要附着在内质网上，但以细胞周期依赖性方式重新定位：Cdc48p在G1晚期进入细胞核；VCP在有丝分裂期间聚集在中心体。Cdc48p的核输入信号序列位于氨基末端附近，其功能通过诱变得到证实。核输入受羧基末端附近酪氨酸残基的细胞周期依赖性磷酸化调节。双杂交研究表明，磷酸化导致蛋白质构象改变，暴露出先前被一段酸性残基掩盖的核输入信号序列。
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