|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
8
|
|
pubmed:dateCreated |
2010-2-15
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
E3 ubiquitin ligases catalyze the final step of ubiquitin conjugation and regulate numerous cellular processes. The HECT class of E3 ubiquitin (Ub) ligases directly transfers Ub from bound E2 enzyme to a myriad of substrates. The catalytic domain of HECT Ub ligases has a bilobal architecture that separates the E2 binding region and catalytic site. An important question regarding HECT domain function is the control of ligase activity and specificity. Here we present a functional analysis of the HECT domain of the E3 ligase HUWE1 based on crystal structures and show that a single N-terminal helix significantly stabilizes the HECT domain. We observe that this element modulates HECT domain activity, as measured by self-ubiquitination induced in the absence of this helix, as distinct from its effects on Ub conjugation of substrate Mcl-1. Such subtle changes to the protein may be at the heart of the vast spectrum of substrate specificities displayed by HECT domain E3 ligases.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-10558980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-11395416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-12535537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-14966115,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-15989956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-15989957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-16061177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-16142244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-16267559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-16269333,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-16341092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-16710298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-16753028,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-17452350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-17567951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-17719543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-17873885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-18022362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-18047743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-18213395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-18488021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-18556554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-18598940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-18923429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-18997778,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-19256548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-19273841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-19359577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20007713-19713937
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
1083-351X
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
19
|
|
pubmed:volume |
285
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
5664-73
|
|
pubmed:dateRevised |
2011-7-25
|
|
pubmed:meshHeading |
pubmed-meshheading:20007713-Catalytic Domain,
pubmed-meshheading:20007713-Crystallography, X-Ray,
pubmed-meshheading:20007713-Humans,
pubmed-meshheading:20007713-Protein Structure, Secondary,
pubmed-meshheading:20007713-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:20007713-Substrate Specificity,
pubmed-meshheading:20007713-Ubiquitin,
pubmed-meshheading:20007713-Ubiquitin-Protein Ligases,
pubmed-meshheading:20007713-Ubiquitination
|
|
pubmed:year |
2010
|
|
pubmed:articleTitle |
A structural element within the HUWE1 HECT domain modulates self-ubiquitination and substrate ubiquitination activities.
|
|
pubmed:affiliation |
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
|
