Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2.

MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2. 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
  • MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2. Abstract Text:

    yetao jinYetao Jin,shelya x zengShelya X Zeng,xiao-xin sunXiao-Xin Sun,hunjoo leeHunjoo Lee,christine blattnerChristine Blattner,zhixiong xiaoZhixiong Xiao,hua luHua Lu,yetao jinYetao Jin,shelya x zengShelya X Zeng,xiao-xin sunXiao-Xin Sun,hunjoo leeHunjoo Lee,christine blattnerChristine Blattner,zhixiong xiaoZhixiong Xiao,hua luHua Lu,

    We have shown previously that MDM2 promotes the degradation of the cyclin-dependent kinase inhibitor p21 through a ubiquitin-independent proteolytic pathway. Here we report that the MDM2 analog, MDMX, also displays a similar activity. MDMX directly bound to p21 and mediated its proteasomal degradation. Although the MDMX effect was independent of MDM2, they synergistically promoted p21 degradation when coexpressed in cells. This degradation appears to be mediated by the 26S proteasome, as MDMX and p21 bound to S2, one of the subunits of the 19S component of the 26S proteasome, in vivo. Conversely, knockdown of MDMX induced the level of endogenous p21 proteins that no longer cofractionated with 26S proteasome, resulting in G(1) arrest. The level of p21 was low at early S phase but markedly induced by knocking down either MDMX or MDM2 in human cells. Ablation of p21 rescued the G(1) arrest caused by double depletion of MDM2 and MDMX in p53-null cells. These results demonstrate that MDMX and MDM2 independently and cooperatively regulate the proteasome-mediated degradation of p21 at the G(1) and early S phases.

    MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2. Publishing Authors By Initials

    y jinY Jin,sx zengSX Zeng,xx sunXX Sun,h leeH Lee,c blattnerC Blattner,z xiaoZ Xiao,h luH Lu,y jinY Jin,sx zengSX Zeng,xx sunXX Sun,h leeH Lee,c blattnerC Blattner,z xiaoZ Xiao,h luH Lu,

    For similar abstracts research abstracts see: abstracts research

    PUBMED ID PMID:

    MEDLINE DATE:

    MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Molecular and cellular biology

    VOLUME: 28

    Page Numbers: 1218-29

    Journal Abbreviation: Mol. Cell. Biol.

    ISSN: 1098-5549

    DAY: 17

    MONTH: 12

    YEAR: 2007

    MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 8109087

    MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2. Keywords Mesh Terms:

    KEYWORDS:

    MESH TERMS:

    Chemical & Substance for Abstract: MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2. Information

    Substance Name:

    Registry Number:

    Grant and Affiliation Information for MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2.

    AFFILIATION: Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Dr., MS4053, Indianapolis, IN 46202, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NCI

    GRANT: CA93614

    ACRONYM: CA

    MEDLINETA: Mol Cell Biol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    MDMX promotes proteasomal turnover of p21 at G1 and early S phases independently of, but in cooperation with, MDM2 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