Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Ubiquitin receptor proteins hHR23a and hPLIC2 interact.

Ubiquitin receptor proteins hHR23a and hPLIC2 interact. 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
  • Ubiquitin receptor proteins hHR23a and hPLIC2 interact. Abstract Text:

    yang kangYang Kang,naixia zhangNaixia Zhang,deanna m koeppDeanna M Koepp,kylie j waltersKylie J Walters,

    Ubiquitin receptor proteins play an important role in delivering ubiquitylated protein substrates to the proteasome for degradation. HHR23a and hPLIC2 are two such ubiquitin receptors that contain ubiquitin-like (UBL) domains, which interact with the proteasome, and ubiquitin-associated (UBA) domains, which interact with ubiquitin. Depending on their abundance UBL/UBA family members can either promote or inhibit the degradation of other proteins, which suggests their participation in the delivery of substrates to the proteasome is highly regulated. In previous work, we determined UBL/UBA domain interactions to promote intramolecular interactions in hHR23a that are abrogated with the addition of either ubiquitin or the proteasome component S5a. In yeast, we determined the hHR23a ortholog (Rad23) to interact with another UBL/UBA family member (Ddi1) and to bind a common tetraubiquitin chain. Here, we use NMR spectroscopy to reveal that hHR23a interacts with hPLIC2 via UBL/UBA domain interactions and to map their binding surfaces. In addition, we demonstrate that these two proteins associate in mammalian cells. Intriguingly, inhibition of the proteasome mitigates hHR23a/hPLIC2 interaction.

    Ubiquitin receptor proteins hHR23a and hPLIC2 interact. Publishing Authors By Initials

    y kangY Kang,n zhangN Zhang,dm koeppDM Koepp,kj waltersKJ Walters,

    For similar proteins: ubiquitins research abstracts see: proteins: ubiquitins research

    PUBMED ID PMID:

    MEDLINE DATE:

    Ubiquitin receptor proteins hHR23a and hPLIC2 interact. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Journal of molecular biology

    VOLUME: 365

    Page Numbers: 1093-101

    Journal Abbreviation: J. Mol. Biol.

    ISSN: 0022-2836

    DAY: 21

    MONTH: 10

    YEAR: 2006

    Ubiquitin receptor proteins hHR23a and hPLIC2 interact. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985088

    Ubiquitin receptor proteins hHR23a and hPLIC2 interact. Keywords Mesh Terms:

    KEYWORDS: Ubiquitins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Ubiquitin receptor proteins hHR23a and hPLIC2 interact. Information

    Substance Name: Proteasome Endopeptidase Complex

    Registry Number: EC 3.4.25.1

    Grant and Affiliation Information for Ubiquitin receptor proteins hHR23a and hPLIC2 interact.

    AFFILIATION: Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NCI

    GRANT: R01 CA097004-04

    ACRONYM: CA

    MEDLINETA: J Mol Biol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Ubiquitin receptor proteins hHR23a and hPLIC2 interact 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