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

Toshinori Matsui, Takashi Watanabe, Kenji Matsuzawa, Mai Kakeno, Nobumasa Okumura, Ikuko Sugiyama, Norimichi Itoh, Kozo Kaibuchi

研究成果: ジャーナルへの寄稿記事

12 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)751-761
ページ数11
ジャーナルMolecular biology of the cell
26
発行部数4
DOI
出版物ステータス出版済み - 2 15 2015

Fingerprint

trans-Golgi Network
Cell Polarity
Phosphorylation
Golgi Apparatus
Microtubules
Proteins
Epithelial Cells
Maintenance

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

これを引用

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.

:: Molecular biology of the cell, 巻 26, 番号 4, 15.02.2015, p. 751-761.

研究成果: ジャーナルへの寄稿記事

Matsui, T, Watanabe, T, Matsuzawa, K, Kakeno, M, Okumura, N, Sugiyama, I, Itoh, N & Kaibuchi, K 2015, 'PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity', Molecular biology of the cell, 巻. 26, 番号 4, pp. 751-761. https://doi.org/10.1091/mbc.E14-09-1382
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. :: Molecular biology of the cell. 2015 ; 巻 26, 番号 4. pp. 751-761.
@article{eec4556f920841418337dff289365ab3,
title = "PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity",
abstract = "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.",
author = "Toshinori Matsui and Takashi Watanabe and Kenji Matsuzawa and Mai Kakeno and Nobumasa Okumura and Ikuko Sugiyama and Norimichi Itoh and Kozo Kaibuchi",
year = "2015",
month = "2",
day = "15",
doi = "10.1091/mbc.E14-09-1382",
language = "English",
volume = "26",
pages = "751--761",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "4",

}

TY - JOUR

T1 - PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity

AU - Matsui, Toshinori

AU - Watanabe, Takashi

AU - Matsuzawa, Kenji

AU - Kakeno, Mai

AU - Okumura, Nobumasa

AU - Sugiyama, Ikuko

AU - Itoh, Norimichi

AU - Kaibuchi, Kozo

PY - 2015/2/15

Y1 - 2015/2/15

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84922796125&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84922796125&partnerID=8YFLogxK

U2 - 10.1091/mbc.E14-09-1382

DO - 10.1091/mbc.E14-09-1382

M3 - Article

C2 - 25518939

AN - SCOPUS:84922796125

VL - 26

SP - 751

EP - 761

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 4

ER -