Caenorhabditis elegans fidgetin homolog FIGL-1, a nuclear-localized AAA ATPase, binds to SUMO

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• 作者：Akinobu Onitake ; Kunitoshi Yamanaka ; Masatoshi Esaki ; Teru Ogura
• 关键词：AAA chaperone ; Caenorhabditis elegans ; Fidgetin ; SUMO ; Ubiquitin
• 刊名：Journal of Structural Biology
• 出版年：2012
• 出版时间：August, 2012
• 年：2012
• 卷：179
• 期：2
• 页码：143-151
• 全文大小：1248 K

文摘

Fidgetin is a member of the AAA (ATPases associated with diverse cellular activities) chaperones. It is well-known that the specific function of a given AAA protein primarily depends upon its subcellular localization and interacting partners. FIGL-1, a Caenorhabditis elegans homolog of mammalian fidgetin, is localized in the nucleus. Here, we identified that the N-terminal PKRVK sequence of FIGL-1 functions as a monopartite nuclear localization signal. Nuclear localization of FIGL-1 is required for its function. We also found that FIGL-1 specifically interacted with SMO-1, a C. elegans homolog of small ubiquitin-like modifier (SUMO), using a yeast two-hybrid assay. Furthermore, the direct physical interaction between FIGL-1 and SMO-1 was demonstrated by pull-down assay using purified proteins as well as immunoprecipitation assay using lysates from epitope-tagged SMO-1-expressing worms. Binding of FIGL-1 to SMO-1 is required for its function. The depletion of FIGL-1 and SMO-1 resulted in developmental defects in C. elegans. Taken altogether, our results indicate that FIGL-1 is a nuclear protein and that in concert with SMO-1, FIGL-1 plays an important role in the regulation of C. elegans development.