English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
 Local TagsRelease HistoryDetailsSummary
  Cbl promotes clustering of endocytic adaptor proteins

Jozik, D., Cárdenes, N., Deribe, Y. L., Moncalián, G., Hoeller, D., Groemping, Y., et al. (2005). Cbl promotes clustering of endocytic adaptor proteins. Nature Structural and Molecular Biology, 12(11), 972-979. doi:10.1038/nsmb1000.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-C1C2-8 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-C1C3-6
Genre: Journal Article
Alternative Title : Cbl promotes clustering of endocytic adaptor proteins

Files

show Files
hide Files
:
NatStructMolBiol_12_2005_972.pdf (Any fulltext), 465KB
 
File Permalink:
-
Name:
NatStructMolBiol_12_2005_972.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://www.nature.com/nsmb/journal/v12/n11/pdf/nsmb1000.pdf (Any fulltext)
Description:
-
OA-Status:
Locator:
https://dx.doi.org/10.1038/nsmb1000 (Any fulltext)
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Jozik, Daniela, Author
Cárdenes, Nayra, Author
Deribe, Yonathan Lissanu, Author
Moncalián, Gabriel, Author
Hoeller, Daniela, Author
Groemping, Yvonne1, Author           
Dikic, Ivan, Author
Rittinger, Katrin2, Author           
Bravo, Jerónimo, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: The ubiquitin ligases c-Cbl and Cbl-b play a crucial role in receptor downregulation by mediating multiple monoubiquitination of receptors and promoting their sorting for lysosomal degradation. Their function is modulated through interactions with regulatory proteins including CIN85 and PIX, which recognize a proline-arginine motif in Cbl and thus promote or inhibit receptor endocytosis. We report the structures of SH3 domains of CIN85 and beta-PIX in complex with a proline-arginine peptide from Cbl-b. Both structures reveal a heterotrimeric complex containing two SH3 domains held together by a single peptide. Trimerization also occurs in solution and is facilitated by the pseudo-symmetrical peptide sequence. Moreover, ternary complexes of CIN85 and Cbl are formed in vivo and are important for the ability of Cbl to promote epidermal growth factor receptor (EGFR) downregulation. These results provide molecular explanations for a novel mechanism by which Cbl controls receptor downregulation.

Details

show
hide
Language(s): eng - English
 Dates: 2005-06-032005-09-132005-10-092005-11-01
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665513
DOI: 10.1038/nsmb1000
URI: http://www.ncbi.nlm.nih.gov/pubmed/16228008
URI: http://www.nature.com/nsmb/journal/v12/n11/full/nsmb1000.html
Other: 6480
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Structural and Molecular Biology
  Other : Nature Struct Biol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: New York, NY : Nature Pub. Group
Pages: - Volume / Issue: 12 (11) Sequence Number: - Start / End Page: 972 - 979 Identifier: ISSN: 1545-9993
CoNE: https://pure.mpg.de/cone/journals/resource/954925603763