The role of karyopherins in the regulated sumoylation of septins.
The role of karyopherins in the regulated sumoylation of septins.
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DOI：
10.1083/jcb.200608066
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发表时间：
2007-04-09
影响因子：
7.8
通讯作者：
Wozniak, Richard W
中科院分区：
文献类型：
--
作者：
Makhnevych, Taras;Ptak, Christopher;Lusk, C Patrick;Aitchison, John D;Wozniak, Richard W
在酿酒酵母中，septin环的几种组分在后期被sumoylated，然后在胞质分裂时突然去sumoylated。我们发现，septin sumoylation是由两个酶的sumoylation途径，Siz 1 p和Ulp 1 p，与核运输机械的相互作用。E3连接酶Siz 1 p在间期通过核转运蛋白Kap 95 p输入细胞核。在M期，Siz 1 p通过核转运蛋白Kap 142 p/Msn 5 p从细胞核输出，随后靶向septin环，在那里它参与septin sumoylation。我们还表明，在有丝分裂过程中sumoylated septins的积累依赖于SUMO异肽酶Ulp 1 p与Kap 121 p和Kap 95 p-Kap 60 p以及核孔复合物（NPC）的相互作用。除了在NPC处隔离Ulp 1之外，Kap 121 p还需要在有丝分裂期间将Ulp 1 p靶向至隔蛋白环。我们提出了一个模型，其中Ulp 1 p是维持在NPC间期和有丝分裂过程中与隔蛋白环短暂相互作用。
In the yeast Saccharomyces cerevisiae, several components of the septin ring are sumoylated during anaphase and then abruptly desumoylated at cytokinesis. We show that septin sumoylation is controlled by the interactions of two enzymes of the sumoylation pathway, Siz1p and Ulp1p, with the nuclear transport machinery. The E3 ligase Siz1p is imported into the nucleus by the karyopherin Kap95p during interphase. In M phase, Siz1p is exported from the nucleus by the karyopherin Kap142p/Msn5p and subsequently targeted to the septin ring, where it participates in septin sumoylation. We also show that the accumulation of sumoylated septins during mitosis is dependent on the interactions of the SUMO isopeptidase Ulp1p with Kap121p and Kap95p–Kap60p and the nuclear pore complex (NPC). In addition to sequestering Ulp1 at the NPC, Kap121p is required for targeting Ulp1p to the septin ring during mitosis. We present a model in which Ulp1p is maintained at the NPC during interphase and transiently interacts with the septin ring during mitosis.