In vivo interaction of AF-6 with activated Ras and ZO-1

Takaharu Yamamoto, Naozumi Harada, Yoji Kawano, Shinichiro Taya, Kozo Kaibuchi

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

AF-6 contains two putative Ras-associating domains (RA domains) which are seen in several Ras effecters such as RalGDS and RIN1. We previously showed that an AF-6 fragment containing the amino-terminal (N-terminal) RA domain directly binds to activated Ras and ZO-1 in vitro. In this study, we showed that a single amino acid mutation in the N-terminal RA domain of AF-6 abolished the interaction of AF-6 with activated Ras and that the sites of this critical amino acid residue were similar to those for Raf-1 and RalGDS. The overexpression of the N-terminal RA domain of AF-6 inhibited the Ras-dependent c-fos promoter/enhancer stimulation in NIH3T3 cells. Endogenous AF-6 was coimmunoprecipitated with activated Ras from Rat1 cells expressing activated Ras. Moreover, we showed that AF-6 was coimmunoprecipitated with ZO-1 from Rat1 cells. Taken together, these results indicate that the Ras-interacting region on AF-6 is structurally similar to that on Raf-1 and on RalGDS and that AF-6 interacts with activated Ras and ZO-1 in vivo.

Original languageEnglish
Pages (from-to)103-107
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume259
Issue number1
DOIs
Publication statusPublished - 27-05-1999
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'In vivo interaction of AF-6 with activated Ras and ZO-1'. Together they form a unique fingerprint.

  • Cite this