Possible role of cortactin phosphorylation by protein kinase Cα in actin-bundle formation at growth cone

Hiroshi Yamada, Tatsuya Kikuchi, Toshio Masumoto, Fan Yan Wei, Tadashi Abe, Tetsuya Takeda, Tei-ichi Nishiki, Kazuhito Tomizawa, Masami Watanabe, Hideki Matsui, Kohji Takei

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Background Information: Cortactin contributes to growth cone morphogenesis by forming with dynamin, ring-shaped complexes that mechanically bundle and stabilise F-actin. However, the regulatory mechanism of cortactin action is poorly understood. Results: Immunofluorescence microscopy revealed that protein kinase C (PKC) α colocalises with cortactin at growth cone filopodia in SH-SY5Y neuroblastoma cells. PKC activation by phorbol 12-myristate 13-acetate causes cortactin phosphorylation, filopodial retraction and F-actin-bundle loss. Moreover, PKCα directly phosphorylates cortactin in vitro at S135/T145/S172, mitigating both cortactin's actin-binding and actin-crosslinking activity, whereas cellular expression of a phosphorylation-mimetic cortactin mutant hinders filopodial formation with a significant decrease of actin bundles. Conclusions: Our results indicate that PKC-mediated cortactin phosphorylation might be implicated in the maintenance of growth cone.

Original languageEnglish
Pages (from-to)319-330
Number of pages12
JournalBiology of the Cell
Volume107
Issue number9
DOIs
Publication statusPublished - Sep 1 2015

Fingerprint

Cortactin
Growth Cones
Protein Kinase C
Actins
Phosphorylation
S 135
Dynamins
Pseudopodia
Neuroblastoma
Morphogenesis
Fluorescence Microscopy
Acetates
Maintenance

Keywords

  • Actin bundle
  • Cortactin
  • Growth cone
  • Protein kinase C

ASJC Scopus subject areas

  • Cell Biology

Cite this

Possible role of cortactin phosphorylation by protein kinase Cα in actin-bundle formation at growth cone. / Yamada, Hiroshi; Kikuchi, Tatsuya; Masumoto, Toshio; Wei, Fan Yan; Abe, Tadashi; Takeda, Tetsuya; Nishiki, Tei-ichi; Tomizawa, Kazuhito; Watanabe, Masami; Matsui, Hideki; Takei, Kohji.

In: Biology of the Cell, Vol. 107, No. 9, 01.09.2015, p. 319-330.

Research output: Contribution to journalArticle

Yamada, Hiroshi ; Kikuchi, Tatsuya ; Masumoto, Toshio ; Wei, Fan Yan ; Abe, Tadashi ; Takeda, Tetsuya ; Nishiki, Tei-ichi ; Tomizawa, Kazuhito ; Watanabe, Masami ; Matsui, Hideki ; Takei, Kohji. / Possible role of cortactin phosphorylation by protein kinase Cα in actin-bundle formation at growth cone. In: Biology of the Cell. 2015 ; Vol. 107, No. 9. pp. 319-330.
@article{0f49fa88fdff4f8a96ca18b2eee2e0b4,
title = "Possible role of cortactin phosphorylation by protein kinase Cα in actin-bundle formation at growth cone",
abstract = "Background Information: Cortactin contributes to growth cone morphogenesis by forming with dynamin, ring-shaped complexes that mechanically bundle and stabilise F-actin. However, the regulatory mechanism of cortactin action is poorly understood. Results: Immunofluorescence microscopy revealed that protein kinase C (PKC) α colocalises with cortactin at growth cone filopodia in SH-SY5Y neuroblastoma cells. PKC activation by phorbol 12-myristate 13-acetate causes cortactin phosphorylation, filopodial retraction and F-actin-bundle loss. Moreover, PKCα directly phosphorylates cortactin in vitro at S135/T145/S172, mitigating both cortactin's actin-binding and actin-crosslinking activity, whereas cellular expression of a phosphorylation-mimetic cortactin mutant hinders filopodial formation with a significant decrease of actin bundles. Conclusions: Our results indicate that PKC-mediated cortactin phosphorylation might be implicated in the maintenance of growth cone.",
keywords = "Actin bundle, Cortactin, Growth cone, Protein kinase C",
author = "Hiroshi Yamada and Tatsuya Kikuchi and Toshio Masumoto and Wei, {Fan Yan} and Tadashi Abe and Tetsuya Takeda and Tei-ichi Nishiki and Kazuhito Tomizawa and Masami Watanabe and Hideki Matsui and Kohji Takei",
year = "2015",
month = "9",
day = "1",
doi = "10.1111/boc.201500032",
language = "English",
volume = "107",
pages = "319--330",
journal = "Biology of the Cell",
issn = "0248-4900",
publisher = "Portland Press Ltd.",
number = "9",

}

TY - JOUR

T1 - Possible role of cortactin phosphorylation by protein kinase Cα in actin-bundle formation at growth cone

AU - Yamada, Hiroshi

AU - Kikuchi, Tatsuya

AU - Masumoto, Toshio

AU - Wei, Fan Yan

AU - Abe, Tadashi

AU - Takeda, Tetsuya

AU - Nishiki, Tei-ichi

AU - Tomizawa, Kazuhito

AU - Watanabe, Masami

AU - Matsui, Hideki

AU - Takei, Kohji

PY - 2015/9/1

Y1 - 2015/9/1

N2 - Background Information: Cortactin contributes to growth cone morphogenesis by forming with dynamin, ring-shaped complexes that mechanically bundle and stabilise F-actin. However, the regulatory mechanism of cortactin action is poorly understood. Results: Immunofluorescence microscopy revealed that protein kinase C (PKC) α colocalises with cortactin at growth cone filopodia in SH-SY5Y neuroblastoma cells. PKC activation by phorbol 12-myristate 13-acetate causes cortactin phosphorylation, filopodial retraction and F-actin-bundle loss. Moreover, PKCα directly phosphorylates cortactin in vitro at S135/T145/S172, mitigating both cortactin's actin-binding and actin-crosslinking activity, whereas cellular expression of a phosphorylation-mimetic cortactin mutant hinders filopodial formation with a significant decrease of actin bundles. Conclusions: Our results indicate that PKC-mediated cortactin phosphorylation might be implicated in the maintenance of growth cone.

AB - Background Information: Cortactin contributes to growth cone morphogenesis by forming with dynamin, ring-shaped complexes that mechanically bundle and stabilise F-actin. However, the regulatory mechanism of cortactin action is poorly understood. Results: Immunofluorescence microscopy revealed that protein kinase C (PKC) α colocalises with cortactin at growth cone filopodia in SH-SY5Y neuroblastoma cells. PKC activation by phorbol 12-myristate 13-acetate causes cortactin phosphorylation, filopodial retraction and F-actin-bundle loss. Moreover, PKCα directly phosphorylates cortactin in vitro at S135/T145/S172, mitigating both cortactin's actin-binding and actin-crosslinking activity, whereas cellular expression of a phosphorylation-mimetic cortactin mutant hinders filopodial formation with a significant decrease of actin bundles. Conclusions: Our results indicate that PKC-mediated cortactin phosphorylation might be implicated in the maintenance of growth cone.

KW - Actin bundle

KW - Cortactin

KW - Growth cone

KW - Protein kinase C

UR - http://www.scopus.com/inward/record.url?scp=84940613016&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84940613016&partnerID=8YFLogxK

U2 - 10.1111/boc.201500032

DO - 10.1111/boc.201500032

M3 - Article

C2 - 26033110

AN - SCOPUS:84940613016

VL - 107

SP - 319

EP - 330

JO - Biology of the Cell

JF - Biology of the Cell

SN - 0248-4900

IS - 9

ER -