Source:http://linkedlifedata.com/resource/pubmed/id/19616115
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
2009-11-2
|
pubmed:abstractText |
Mammalian AMP-activated protein kinase (AMPK) is a heterotrimeric serine/threonine protein kinase that acts as a sensor of cellular energy status. It interacts with a great variety of different substrates leading to short-term (i.e. regulation of the activity of different enzymes by direct phosphorylation) and long-term effects (i.e. regulation of transcriptional activity of different transcription factors). In this work, we describe the use of the yeast two-hybrid technology to identify additional proteins that interact with the different subunits of AMPK. We have performed three yeast two-hybrid screenings of a human skeletal muscle cDNA library using three different baits: a constitutively active form of AMPKalpha2 (LexA-AMPKalpha2-T172D) co-expressed with AMPKgamma1, LexA-AMPKbeta2 and LexA-AMPKgamma3. Our results identify novel interaction partners of AMPK in human skeletal muscle. We also further characterize the interaction of AMPK with one of these novel interacting proteins, the non-ATPase subunit of the proteasome PSMD11. Our results indicate that AMPK is able to interact physically with this subunit and modify its phosphorylation status, supporting a possible role for AMPK in regulating proteasome function.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
1878-5875
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:volume |
41
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2431-9
|
pubmed:meshHeading |
pubmed-meshheading:19616115-AMP-Activated Protein Kinases,
pubmed-meshheading:19616115-Cell Line,
pubmed-meshheading:19616115-Cloning, Molecular,
pubmed-meshheading:19616115-Humans,
pubmed-meshheading:19616115-Multiprotein Complexes,
pubmed-meshheading:19616115-Muscle Fibers, Skeletal,
pubmed-meshheading:19616115-Phosphorylation,
pubmed-meshheading:19616115-Proteasome Endopeptidase Complex,
pubmed-meshheading:19616115-Protein Binding,
pubmed-meshheading:19616115-Transcriptional Activation,
pubmed-meshheading:19616115-Two-Hybrid System Techniques
|
pubmed:year |
2009
|
pubmed:articleTitle |
Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase.
|
pubmed:affiliation |
Instituto de Biomedicina de Valencia, CSIC and CIBER de Enfermedades Raras (CIBERER), Jaime Roig 11, 46010 Valencia, Spain.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|