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PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity
The organization of the Golgi apparatus is essential for cell polarization and its maintenance. The polarity regulator PAR complex (PAR3, PAR6, and aPKC) plays critical roles in several processes of cell polarization. However, how the PAR complex participates in regulating the organization of the Go...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4325844/ https://www.ncbi.nlm.nih.gov/pubmed/25518939 http://dx.doi.org/10.1091/mbc.E14-09-1382 |
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author | Matsui, Toshinori Watanabe, Takashi Matsuzawa, Kenji Kakeno, Mai Okumura, Nobumasa Sugiyama, Ikuko Itoh, Norimichi Kaibuchi, Kozo |
author_facet | Matsui, Toshinori Watanabe, Takashi Matsuzawa, Kenji Kakeno, Mai Okumura, Nobumasa Sugiyama, Ikuko Itoh, Norimichi Kaibuchi, Kozo |
author_sort | Matsui, Toshinori |
collection | PubMed |
description | The organization of the Golgi apparatus is essential for cell polarization and its maintenance. The polarity regulator PAR complex (PAR3, PAR6, and aPKC) plays critical roles in several processes of cell polarization. However, how the PAR complex participates in regulating the organization of the Golgi remains largely unknown. Here we demonstrate the functional cross-talk of the PAR complex with CLASP2, which is a microtubule plus-end–tracking protein and is involved in organizing the Golgi ribbon. CLASP2 directly interacted with PAR3 and was phosphorylated by aPKC. In epithelial cells, knockdown of either PAR3 or aPKC induced the aberrant accumulation of CLASP2 at the trans-Golgi network (TGN) concomitantly with disruption of the Golgi ribbon organization. The expression of a CLASP2 mutant that inhibited the PAR3-CLASP2 interaction disrupted the organization of the Golgi ribbon. 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. On the basis of these observations, we propose that PAR3 and aPKC control the organization of the Golgi through CLASP2 phosphorylation. |
format | Online Article Text |
id | pubmed-4325844 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-43258442015-04-30 PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity Matsui, Toshinori Watanabe, Takashi Matsuzawa, Kenji Kakeno, Mai Okumura, Nobumasa Sugiyama, Ikuko Itoh, Norimichi Kaibuchi, Kozo Mol Biol Cell Articles The organization of the Golgi apparatus is essential for cell polarization and its maintenance. The polarity regulator PAR complex (PAR3, PAR6, and aPKC) plays critical roles in several processes of cell polarization. However, how the PAR complex participates in regulating the organization of the Golgi remains largely unknown. Here we demonstrate the functional cross-talk of the PAR complex with CLASP2, which is a microtubule plus-end–tracking protein and is involved in organizing the Golgi ribbon. CLASP2 directly interacted with PAR3 and was phosphorylated by aPKC. In epithelial cells, knockdown of either PAR3 or aPKC induced the aberrant accumulation of CLASP2 at the trans-Golgi network (TGN) concomitantly with disruption of the Golgi ribbon organization. The expression of a CLASP2 mutant that inhibited the PAR3-CLASP2 interaction disrupted the organization of the Golgi ribbon. 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. On the basis of these observations, we propose that PAR3 and aPKC control the organization of the Golgi through CLASP2 phosphorylation. The American Society for Cell Biology 2015-02-15 /pmc/articles/PMC4325844/ /pubmed/25518939 http://dx.doi.org/10.1091/mbc.E14-09-1382 Text en © 2015 Matsui et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Matsui, Toshinori Watanabe, Takashi Matsuzawa, Kenji Kakeno, Mai Okumura, Nobumasa Sugiyama, Ikuko Itoh, Norimichi Kaibuchi, Kozo PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity |
title | PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity |
title_full | PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity |
title_fullStr | PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity |
title_full_unstemmed | PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity |
title_short | PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity |
title_sort | par3 and apkc regulate golgi organization through clasp2 phosphorylation to generate cell polarity |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4325844/ https://www.ncbi.nlm.nih.gov/pubmed/25518939 http://dx.doi.org/10.1091/mbc.E14-09-1382 |
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