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  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.

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

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NatStructMolBiol_12_2005_972.pdf (Any fulltext), 465KB
 
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 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              

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 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.

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Language(s): eng - English
 Dates: 2005-06-032005-09-132005-10-092005-11-01
 Publication Status: Published in print
 Pages: 8
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 Table of Contents: -
 Rev. Method: Peer
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Title: Nature Structural and Molecular Biology
  Other : Nature Struct Biol
Source Genre: Journal
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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: /journals/resource/954925603763