Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 179, Issue 2, Pages 143-151Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2012.04.022
Keywords
AAA chaperone; Caenorhabditis elegans; Fidgetin; SUMO; Ubiquitin
Funding
- Ministry of Education, Culture, Science, Sports and Technology, Japan
- Kurnamoto University Global COE Program Cell Fate Regulation Research and Education Unit
- Grants-in-Aid for Scientific Research [24770189, 19058012] Funding Source: KAKEN
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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. (C) 2012 Elsevier Inc. All rights reserved.
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