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Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains

EMBO reports, 2009-05, Vol.10 (5), p.466-473 [Peer Reviewed Journal]

Copyright © 2009 European Molecular Biology Organization ;Copyright © 2009, European Molecular Biology Organization 2009 ;ISSN: 1469-221X ;EISSN: 1469-3178 ;DOI: 10.1038/embor.2009.55 ;PMID: 19373254 ;CODEN: ERMEAX

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Title:
Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
Author: Komander, David ; Reyes-Turcu, Francisca ; Licchesi, Julien D F ; Odenwaelder, Peter ; Wilkinson, Keith D ; Barford, David
Subjects: Binding sites ; Cellular biology ; Crystallography, X-Ray ; deubiquitinase ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Endopeptidases - chemistry ; Endopeptidases - metabolism ; Lysine - chemistry ; Models, Molecular ; Molecular biology ; NF-κB signalling ; Polyubiquitin - chemistry ; Polyubiquitin - metabolism ; Protein Binding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins ; Scientific Report ; Signal transduction ; TAK1/IKK/NEMO/NF-κB ; ubiquitin binding domain ; ubiquitin linkage
Is Part Of: EMBO reports, 2009-05, Vol.10 (5), p.466-473
Description: At least eight types of ubiquitin chain exist, and individual linkages affect distinct cellular processes. The only distinguishing feature of differently linked ubiquitin chains is their structure, as polymers of the same unit are chemically identical. Here, we have crystallized Lys 63‐linked and linear ubiquitin dimers, revealing that both adopt equivalent open conformations, forming no contacts between ubiquitin molecules and thereby differing significantly from Lys 48‐linked ubiquitin chains. We also examined the specificity of various deubiquitinases (DUBs) and ubiquitin‐binding domains (UBDs). All analysed DUBs, except CYLD, cleave linear chains less efficiently compared with other chain types, or not at all. Likewise, UBDs can show chain specificity, and are able to select distinct linkages from a ubiquitin chain mixture. We found that the UBAN (ubiquitin binding in ABIN and NEMO) motif of NEMO (NF‐κB essential modifier) binds to linear chains exclusively, whereas the NZF (Npl4 zinc finger) domain of TAB2 (TAK1 binding protein 2) is Lys 63 specific. Our results highlight remarkable specificity determinants within the ubiquitin system.
Publisher: Chichester, UK: John Wiley & Sons, Ltd
Language: English
Identifier: ISSN: 1469-221X
EISSN: 1469-3178
DOI: 10.1038/embor.2009.55
PMID: 19373254
CODEN: ERMEAX
Source: GFMER Free Medical Journals
MEDLINE
PubMed Central
Alma/SFX Local Collection
ProQuest Central

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Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains

Copyright © 2009 European Molecular Biology Organization ;Copyright © 2009, European Molecular Biology Organization 2009 ;ISSN: 1469-221X ;EISSN: 1469-3178 ;DOI: 10.1038/embor.2009.55 ;PMID: 19373254 ;CODEN: ERMEAX

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