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Regulatory machinery of UNC‐33 Ce‐CRMP localization in neurites during neuronal development in Caenorhabditis elegans
Author(s) -
Tsuboi Daisuke,
Hikita Takao,
Qadota Hiroshi,
Amano Mutsuki,
Kaibuchi Kozo
Publication year - 2005
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2005.03490.x
Subject(s) - caenorhabditis elegans , neurite , neuroscience , biology , microbiology and biotechnology , gene , genetics , in vitro
In Caenorhabditis elegans , unc‐33 encodes an orthologue of the vertebrate collapsin response mediator protein (CRMP) family. We previously reported that CRMP‐2 accumulated in the distal part of the growing axon of vertebrate neurons and played critical roles in axon elongation. unc‐33 mutants show axonal outgrowth defects in several neurons. It has been reported that UNC‐33 accumulates in neurites, whereas a missense mutation causes the mislocalization of UNC‐33 from neurites to cell body, which suggests that the localization of UNC‐33 in neurites is important for axonal outgrowth. However, it is unclear how UNC‐33 accumulates in neurites and regulates neuronal development. In this study, to understand the regulatory mechanisms of localization of UNC‐33 in neurites, we screened for the mutants that were involved in the localization of UNC‐33, and identified three mutants: unc‐14 (RUN domain protein), unc‐51 (ULK kinase) and unc‐116 (kinesin heavy chain). UNC‐14 is known to associate with UNC‐51. UNC‐116 forms a complex with KLC‐2 as Kinesin‐1, a microtubule‐dependent motor complex. We found that UNC‐33 interacted with UNC‐14 and KLC‐2 in vivo . These results suggest that the UNC‐14/UNC‐51 complex and Kinesin‐1 are involved in the localization of UNC‐33 in neurites.