Source:http://linkedlifedata.com/resource/pubmed/id/21143188
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2011-2-11
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pubmed:abstractText |
The TRIM (tripartite motif) family of proteins is characterized by the presence of the tripartite motif module, composed of a RING domain, one or two B-box domains and a coiled-coil region. TRIM proteins are involved in many cellular processes and represent the largest subfamily of RING-containing putative ubiquitin E3 ligases. Whereas their role as E3 ubiquitin ligases has been presumed, and in several cases established, little is known about their specific interactions with the ubiquitin-conjugating E2 enzymes or UBE2s. In the present paper, we report a thorough screening of interactions between the TRIM and UBE2 families. We found a general preference of the TRIM proteins for the D and E classes of UBE2 enzymes, but we also revealed very specific interactions between TRIM9 and UBE2G2, and TRIM32 and UBE2V1/2. Furthermore, we demonstrated that the TRIM E3 activity is only manifest with the UBE2 with which they interact. For most specific interactions, we could also observe subcellular co-localization of the TRIM involved and its cognate UBE2 enzyme, suggesting that the specific selection of TRIM-UBE2 pairs has physiological relevance. Our findings represent the basis for future studies on the specific reactions catalysed by the TRIM E3 ligases to determine the fate of their targets.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TRIM25 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TRIM32 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TRIM9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Conjugating Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1470-8728
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pubmed:author | |
pubmed:copyrightInfo |
© The Authors Journal compilation © 2011 Biochemical Society
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
434
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
309-19
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pubmed:meshHeading |
pubmed-meshheading:21143188-Amino Acid Sequence,
pubmed-meshheading:21143188-Cells, Cultured,
pubmed-meshheading:21143188-HeLa Cells,
pubmed-meshheading:21143188-Humans,
pubmed-meshheading:21143188-Molecular Sequence Data,
pubmed-meshheading:21143188-Nerve Tissue Proteins,
pubmed-meshheading:21143188-Transcription Factors,
pubmed-meshheading:21143188-Ubiquitin-Conjugating Enzymes,
pubmed-meshheading:21143188-Ubiquitin-Protein Ligases
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pubmed:year |
2011
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pubmed:articleTitle |
Functional interactions between ubiquitin E2 enzymes and TRIM proteins.
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pubmed:affiliation |
Cluster in Biomedicine (CBM), AREA Science Park, s.s. 14 km 163.5 Basovizza, 34149 Trieste, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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