Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit.

Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit. Abstract Text:

    kazunobu saitoKazunobu Saito,kengo enyaKengo Enya,chitose oneyamaChitose Oneyama,tomoya hikitaTomoya Hikita,masato okadaMasato Okada,kazunobu saitoKazunobu Saito,kengo enyaKengo Enya,chitose oneyamaChitose Oneyama,tomoya hikitaTomoya Hikita,masato okadaMasato Okada,

    To elucidate the regulatory mechanism of cell transformation induced by c-Src tyrosine kinase, we performed a proteomic analysis of tyrosine phosphorylated proteins that interact with c-Src and/or its negative regulator Csk. The c-Src interacting proteins were affinity-purified from Src transformed cells using the Src SH2 domain as a ligand. LC-MS/MS analysis of the purified proteins identified general Src substrates, such as focal adhesion kinase and paxillin, and ZO-1/2 as a transformation-dependent Src target. The Csk binding proteins were analyzed by a tandem affinity purification method. In addition to the previously identified Csk binding proteins, including Cbp/PAG, paxillin, and caveolin-1, we found that ZO-1/2 could also serve as a major Csk binding protein. ZO-2 was phosphorylated concurrently with Src transformation and specifically bound to Csk in a Csk SH2 dependent manner. These results suggest novel roles for ZO proteins as Src/Csk scaffolds potentially involved in the regulation of Src transformation.

    Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit. Publishing Authors By Initials

    k saitoK Saito,k enyaK Enya,c oneyamaC Oneyama,t hikitaT Hikita,m okadaM Okada,k saitoK Saito,k enyaK Enya,c oneyamaC Oneyama,t hikitaT Hikita,m okadaM Okada,

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Biochemical and biophysical research communication

    VOLUME: 366

    Page Numbers: 969-75

    Journal Abbreviation: Biochem. Biophys. Res. Commun.

    ISSN: 1090-2104

    DAY: 18

    MONTH: 12

    YEAR: 2007

    Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 372516

    Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit. Keywords Mesh Terms:

    KEYWORDS:

    MESH TERMS:

    Chemical & Substance for Abstract: Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit. Information

    Substance Name:

    Registry Number:

    Grant and Affiliation Information for Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit.

    AFFILIATION: Department of Oncogene Research, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: Biochem Biophys Res Commun

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Proteomic identification of ZO-1/2 as a novel scaffold for Src/Csk regulatory circuit Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News