Intracellular cAMP controls a physical association of V-1 with CapZ in cultured mammalian endocrine cells

Masashi Kitazawa, Tohru Yamakuni, Si Young Song, Chieko Kato, Reiko Tsuchiya, Mami Ishida, Nobuhide Suzuki, Eijiro Adachi, Shintaro Iwashita, Susumu Ueno, Nobuyuki Yanagihara, Masato Taoka, Toshiaki Isobe, Yasushi Ohizumi

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

V-1, an ankyrin repeat protein with the activity to control tyrosine hydroxylase (TH) gene expression and transmitter release in PC12D cells, associates with CapZ, an actin capping protein, and thereby regulates actin polymerization in vitro. In this study, immunoprecipitation and Western blot analysis showed that V-1 was physically associated with CapZ-β in PC12D transfectants overexpressing V-1. These proteins were co-localized in the soma of Purkinje cells of rat cerebellum as assayed by immunohistochemistry. Furthermore, in the V-1 transfectants, the amount of CapZ which physically associated with V-1 was steeply reduced at 2 h after treatment with forskolin, but was thereafter increased to reach its initial level at 12 h after forskolin-treatment. These results suggest that the association of V-1 with CapZ is controlled by a cAMP-dependent signalling pathway probably to play a functional role in the regulatory mechanism of actin dynamics in the endocrine system and the central nervous system.

Original languageEnglish
Pages (from-to)181-186
Number of pages6
JournalBiochemical and biophysical research communications
Volume331
Issue number1
DOIs
Publication statusPublished - 2005 May 27

Keywords

  • CapZ
  • Physical association
  • V-1 protein
  • cAMP

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Intracellular cAMP controls a physical association of V-1 with CapZ in cultured mammalian endocrine cells'. Together they form a unique fingerprint.

Cite this