RRC ID 46419
Author Onitake A, Yamanaka K, Esaki M, Ogura T.
Title Caenorhabditis elegans fidgetin homolog FIGL-1, a nuclear-localized AAA ATPase, binds to SUMO.
Journal J Struct Biol
Abstract 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.
Volume 179(2)
Pages 143-51
Published 2012-8-1
DOI 10.1016/j.jsb.2012.04.022
PII S1047-8477(12)00136-0
PMID 22575764
MeSH Adenosine Triphosphatases / genetics Adenosine Triphosphatases / metabolism* Animals Caenorhabditis elegans Proteins / genetics Caenorhabditis elegans Proteins / metabolism* Cell Nucleus / metabolism Humans Immunohistochemistry Immunoprecipitation Nuclear Proteins Protein Binding / genetics Protein Binding / physiology SUMO-1 Protein / genetics SUMO-1 Protein / metabolism* Two-Hybrid System Techniques Ubiquitin / genetics Ubiquitin / metabolism
IF 3.754
Times Cited 7
C.elegans tm808