rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 3
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pubmed:dateCreated |
2005-6-6
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pubmed:abstractText |
PKCzeta (protein kinase Czeta) is a serine/threonine protein kinase controlled by insulin, various growth factors and phosphoinositide 3-kinase. It has been implicated in controlling glucose transport in response to insulin by the translocation of GLUT4-(glucose transporter 4) containing vesicles to the plasma membrane in stimulated cells. How PKCzeta modulates GLUT4 vesicle trafficking remains unknown. A yeast two-hybrid screen using full-length human PKCzeta identified 80K-H protein as an interactor with PKCzeta. GST (glutathione S-transferase) pull-down assays with GST-tagged 80K-H constructs confirmed the interaction and showed that the N-terminal portion of 80K-H was not required for the interaction. Immunoprecipitates of endogenous PKCzeta from Cho cells, 3T3-L1 adipocytes or L6 myotubes contained endogenous 80K-H, demonstrating a physiological interaction. Insulin stimulation enhanced the association 3-5-fold. Immunoprecipitates of endogenous 80K-H contained endogenous munc18c and immunoprecipitates of endogenous munc18c contained endogenous PKCzeta, with insulin markedly increasing the amount of co-immunoprecipitated protein in each case. These results show that insulin triggers interactions in vivo between PKCzeta, 80K-H and munc18c. Overexpression of 80K-H constructs mimicked the action of insulin in stimulating both glucose uptake and translocation of Myc-tagged GLUT4 in Cho cells, with the level of effect proportional to the ability of the constructs to associate with munc18c. These results identify 80K-H as a new player involved in GLUT4 vesicle transport and identify a link between a kinase involved in the insulin signalling cascade, PKCzeta, and a known component of the GLUT4 vesicle trafficking pathway, munc18c. The results suggest a model whereby insulin triggers the formation of a PKCzeta-80K-H-munc18c complex that enhances GLUT4 translocation to the plasma membrane.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15707389-10100627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15707389-10394363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15707389-10473560,
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 4,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosidases,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Munc18 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PRKCSH protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Prkcsh protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase C zeta
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1470-8728
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
388
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
785-93
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15707389-Animals,
pubmed-meshheading:15707389-Biological Transport,
pubmed-meshheading:15707389-CHO Cells,
pubmed-meshheading:15707389-COS Cells,
pubmed-meshheading:15707389-Cell Membrane,
pubmed-meshheading:15707389-Cercopithecus aethiops,
pubmed-meshheading:15707389-Cricetinae,
pubmed-meshheading:15707389-Cytoplasmic Vesicles,
pubmed-meshheading:15707389-Glucose,
pubmed-meshheading:15707389-Glucose Transporter Type 4,
pubmed-meshheading:15707389-Glucosidases,
pubmed-meshheading:15707389-Humans,
pubmed-meshheading:15707389-Insulin,
pubmed-meshheading:15707389-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:15707389-Mice,
pubmed-meshheading:15707389-Multiprotein Complexes,
pubmed-meshheading:15707389-Munc18 Proteins,
pubmed-meshheading:15707389-Phosphoproteins,
pubmed-meshheading:15707389-Phosphorylation,
pubmed-meshheading:15707389-Protein Binding,
pubmed-meshheading:15707389-Protein Kinase C,
pubmed-meshheading:15707389-Saccharomyces cerevisiae,
pubmed-meshheading:15707389-Two-Hybrid System Techniques
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pubmed:year |
2005
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pubmed:articleTitle |
Identification of 80K-H as a protein involved in GLUT4 vesicle trafficking.
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pubmed:affiliation |
School of Biological Sciences, University of Southampton, Biomedical Sciences Building, Bassett Crescent East, Southampton SO16 7PX, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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