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PMID: 23747110 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Comment

HHARI is one HECT of a RING.

Structure (London, England : 1993) ·Vol. 21 ·No. 6 ·2013-06-04 ·Pages 872-4

Davies CW, Das C

Abstract

E3 ubiquitin ligases are the last of an enzyme trio that covalently modifies proteins with ubiquitin, facilitating various cellular functions. In this issue of Structure, Duda and colleagues provide the structural basis for the autoinhibited Ariadne-family of E3-ubiquitin ligases.

MeSH Terms
Carrier Proteins/chemistry Humans Ubiquitin-Protein Ligases/chemistry
Chemicals
Carrier Proteins ARIH1 protein, human Ubiquitin-Protein Ligases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Davies Christopher W
Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
Das Chittaranjan
References (4)
4 references, click to expand
  1. RING domain E3 ubiquitin ligases.
    Annu Rev Biochem. 2009;78:399-434 PMID: 19489725
  2. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids.
    Nature. 2011 Jun 2;474(7349):105-8 PMID: 21532592
  3. Structure of parkin reveals mechanisms for ubiquitin ligase activation.
    Science. 2013 Jun 21;340(6139):1451-5 PMID: 23661642
  4. Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism.
    Structure. 2013 Jun 4;21(6):1030-41 PMID: 23707686
Article Info
Journal
Structure (London, England : 1993)
Abbr.
Structure
ISSN
1878-4186
DOI
10.1016/j.str.2013.05.003
Published
2013-06-04
Pages
872-4
Language
English
Region
United States
NLM ID
101087697
PMCID
PMC3972756
Subset
IM
Grants
NIGMS NIH HHS · R01 GM103401 · United States
NCRR NIH HHS · R01 RR026273 · United States
NCRR NIH HHS · 1R01RR026273 · United States
Corrections
CommentOn
PMID: 23707686
External Links
PubMed source DOI: 10.1016/j.str.2013.05.003 PMC Full Text View journal details
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