PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity

• DOI: 10.1091/mbc.e14-09-1382
• Publication Date: 2014-12-18T18:49:51Z
• Authors: Toshinori Matsui; Takashi Watanabe; Kenji Matsuzawa; Mai Kakeno; Nobumasa Okumura; Ikuko Sugiyama; Norimichi Itoh; Kozo Kaibuchi
• Keywords: Polarity (international relations); Cell polarity

The organization of the Golgi apparatus is essential for cell polarization and its maintenance. polarity regulator PAR complex (PAR3, PAR6, aPKC) plays critical roles in several processes polarization. However, how participates regulating remains largely unknown. Here we demonstrate functional cross-talk with CLASP2, which a microtubule plus-end-tracking protein involved organizing ribbon. CLASP2 directly interacted PAR3 was phosphorylated by aPKC. In epithelial cells, knockdown either or aPKC induced aberrant accumulation at trans-Golgi network (TGN) concomitantly disruption ribbon organization. expression mutant that inhibited PAR3-CLASP2 interaction disrupted known to localize TGN through GCC185. This aPKC-mediated phosphorylation CLASP2. Furthermore, nonphosphorylatable enhanced colocalization GCC185, thereby perturbing On basis these observations, propose control phosphorylation.