PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity.
Bottom Line: CLASP2 is known to localize to the TGN through its interaction with the TGN protein GCC185.This interaction was inhibited by the aPKC-mediated phosphorylation of CLASP2.Furthermore, the nonphosphorylatable mutant enhanced the colocalization of CLASP2 with GCC185, thereby perturbing the Golgi organization.
Affiliation: Department of Cell Pharmacology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan.Show MeSH
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Mentions: By comprehensive screening for interactors of PAR3, we previously identified CLASP2 as a candidate interactor (Itoh et al., 2010). We first verified our finding by immunoprecipitating the complex of PAR3 and CLASP2. Endogenous CLASP2 was specifically precipitated with endogenous PAR3 and vice versa (Figure 1A). Furthermore, Myc-fused CLASP2α and CLASP2γ were precipitated with green fluorescent protein (GFP)–fused PAR3 (Figure 1B). CLASP1α was also precipitated with PAR3 (Figure 1C). These results indicate that PAR3 physiologically associates with CLASPs irrespective of its isoforms.
Affiliation: Department of Cell Pharmacology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan.