SUMO regulates the assembly and function of a cytoplasmic intermediate filament protein in C. elegans.

SUMO regulates the assembly and function of a cytoplasmic intermediate filament protein in C. elegans.
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DOI:
10.1016/j.devcel.2009.10.005
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发表时间:
2009-11
期刊:
影响因子:
11.8
通讯作者:
Broday, Limor
Broday, Limor
中科院分区:
生物学1区
文献类型:
--
作者:
Kaminsky, Rachel;Denison, Carilee;Bening-Abu-Shach, Ulrike;Chisholm, Andrew D.;Gygi, Steven P.;Broday, Limor

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类小泛素化是一种可逆的翻译后修饰,在转录调控、细胞分裂、染色体完整性和DNA损伤反应等过程中发挥作用。利用蛋白质组学方法,我们鉴定了约250个C.优美的一个这样的目标是命名为IFB-1的细胞质中间丝(cIF)蛋白,其在蠕虫表皮中的半桥粒样结构中表达,并且对于胚胎伸长和维持肌肉附着于角质层是必需的。在没有SUMO的情况下,IFB-1在侧表皮形成异位丝和蛋白质聚集体。此外,SUMO的耗竭或IFB-1上SUMO受体位点的突变导致其细胞质可溶性池的减少,导致其在表皮附着结构内的交换率降低。这些观察结果表明,SUMO通过维持非聚合IFB-1的细胞质池来调节cIF组装,并且这是正常IFB-1功能所必需的。
Sumoylation is a reversible post-translational modification that plays roles in many processes, including transcriptional regulation, cell division, chromosome integrity and DNA damage response. Using a proteomics approach, we identified ~250 candidate targets of sumoylation in C. elegans. One such target is the cytoplasmic intermediate filament (cIF) protein named IFB-1, which is expressed in hemidesmosome-like structures in the worm epidermis and is essential for embryonic elongation and maintenance of muscle attachment to the cuticle. In the absence of SUMO, IFB-1 formed ectopic filaments and protein aggregates in the lateral epidermis. Moreover, depletion of SUMO or mutation of the SUMO acceptor site on IFB-1 resulted in a reduction of its cytoplasmic soluble pool, leading to a decrease in its exchange rate within epidermal attachment structures. These observations indicate that SUMO regulates cIF assembly by maintaining a cytoplasmic pool of non-polymerized IFB-1, and that this is necessary for normal IFB-1 function.
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