RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly.
RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly.
复制标题
rangap1*Sumo1在有丝分裂的开始时被磷酸化，并在NPC拆卸后仍与RANBP2相关。
DOI：
10.1083/jcb.200309126
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发表时间：
2004-03-29
期刊：
影响因子：
--
通讯作者：
Melchior F
中科院分区：
文献类型：
--
作者：
Swaminathan S;Kiendl F;Körner R;Lupetti R;Hengst L;Melchior F
RanGTP酶激活蛋白RanGAP 1在核质转运和有丝分裂中具有重要功能。在间期，很大一部分脊椎动物SUMO 1修饰的RanGAP 1与核孔蛋白RanBP 2/Nup 358在核孔复合物处形成稳定的复合物。RanBP 2不仅在RanGT循环中起作用，而且还是SUMO 1 E3连接酶。在这里，我们显示RanGAP 1在残基T409，S428和S442上被磷酸化。磷酸化发生在核膜破裂之前，并在整个有丝分裂过程中维持。诺考达唑阻滞导致定量磷酸化。M期激酶cyclin B/Cdk 1在体外有效磷酸化RanGAP 1，T409磷酸化与cyclin B1在体内的核积累相关。我们发现，磷酸化的RanGAP 1仍然与RanBP 2/NUP 358和SUMO E2-共轭酶Ubc 9在有丝分裂，因此有丝分裂磷酸化可能有功能后果的RanGT循环和/或RanBP 2依赖的SUMO化。
The RanGTPase activating protein RanGAP1 has essential functions in both nucleocytoplasmic transport and mitosis. In interphase, a significant fraction of vertebrate SUMO1-modified RanGAP1 forms a stable complex with the nucleoporin RanBP2/Nup358 at nuclear pore complexes. RanBP2 not only acts in the RanGTPase cycle but also is a SUMO1 E3 ligase. Here, we show that RanGAP1 is phosphorylated on residues T409, S428, and S442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis. Nocodazole arrest leads to quantitative phosphorylation. The M-phase kinase cyclin B/Cdk1 phosphorylates RanGAP1 efficiently in vitro, and T409 phosphorylation correlates with nuclear accumulation of cyclin B1 in vivo. We find that phosphorylated RanGAP1 remains associated with RanBP2/Nup358 and the SUMO E2–conjugating enzyme Ubc9 in mitosis, hence mitotic phosphorylation may have functional consequences for the RanGTPase cycle and/or for RanBP2-dependent sumoylation.
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