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: Finally, we performed rescue experiments in CLASP-depleted cells with GFP–CLASP2γ-3A. The expression of the siRNA-resistant wild-type CLASP2γ restored the organization of the Golgi ribbon to that observed in control cells. However, GFP–CLASP2γ-3A failed to restore the organization of the Golgi ribbon (Figure 6, A and B). In addition, compared with the wild type, GFP–CLASP2γ-3A strongly colocalized with GCC185, which was similar to the behavior of endogenous CLASP2 in PAR3- and aPKC-depleted cells (Figures 3B and 6A). These results suggest that PAR3 and aPKC regulate the organization of the Golgi ribbon through the phosphorylation of CLASP2.
Affiliation: Department of Cell Pharmacology, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan.