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- Scopus: eid_2-s2.0-56749173518
- PMID: 18801932
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Article: Regulation of glucose transporter 4 translocation by the rab guanosine triphosphatase-activating protein AS160/TBC1D4: Role of phosphorylation and membrane association
Title | Regulation of glucose transporter 4 translocation by the rab guanosine triphosphatase-activating protein AS160/TBC1D4: Role of phosphorylation and membrane association |
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Authors | |
Issue Date | 2008 |
Publisher | Endocrine Society. The Journal's web site is located at http://mend.endojournals.org/ |
Citation | Molecular Endocrinology, 2008, v. 22 n. 12, p. 2703-2715 How to Cite? |
Abstract | Insulin-stimulated translocation of the glucose transporter GLUT4 to the plasma membrane in muscle and fat cells depends on the phosphatidylinositide 3-kinase/Akt pathway. The downstream target AS160/TBC1D4 is phosphorylated upon insulin stimulation and contains a TBC domain (Tre-2/Bub2/Cdc16) that is present in most Rab guanosine triphosphatase-activating proteins. TBC1D4 associates with GLUT4-containing membranes under basal conditions and dissociates from membranes with insulin. Here we show that the association of TBC1D4 with membranes is required for its inhibitory action on GLUT4 translocation under basal conditions. Whereas the insulin-dependent dissociation of TBC1D4 from membranes was not required for GLUT4 translocation, its phosphorylation was essential. Many agonists that stimulate GLUT4 translocation failed to trigger TBC1D4 translocation to the cytosol, but in most cases these agonists stimulated TBC1D4 phosphorylation at T642, and their effects on GLUT4 translocation were inhibited by overexpression of the TBC1D4 phosphorylation mutant (TBC1D4-4P). We postulate that TBC1D4 acts to impede GLUT4 translocation by disarming a Rab protein found on GLUT4-containing-membranes and that phosphorylation of TBC1D4 per se is sufficient to overcome this effect, allowing GLUT4 translocation to the cell surface to proceed. Copyright © 2008 by The Endocrine Society. |
Persistent Identifier | http://hdl.handle.net/10722/59172 |
ISSN | 2018 Impact Factor: 3.628 2019 SCImago Journal Rankings: 1.676 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Stöckli, J | en_HK |
dc.contributor.author | Davey, JR | en_HK |
dc.contributor.author | HohnenBehrens, C | en_HK |
dc.contributor.author | Xu, A | en_HK |
dc.contributor.author | James, DE | en_HK |
dc.contributor.author | Ramm, G | en_HK |
dc.date.accessioned | 2010-05-31T03:44:17Z | - |
dc.date.available | 2010-05-31T03:44:17Z | - |
dc.date.issued | 2008 | en_HK |
dc.identifier.citation | Molecular Endocrinology, 2008, v. 22 n. 12, p. 2703-2715 | en_HK |
dc.identifier.issn | 0888-8809 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/59172 | - |
dc.description.abstract | Insulin-stimulated translocation of the glucose transporter GLUT4 to the plasma membrane in muscle and fat cells depends on the phosphatidylinositide 3-kinase/Akt pathway. The downstream target AS160/TBC1D4 is phosphorylated upon insulin stimulation and contains a TBC domain (Tre-2/Bub2/Cdc16) that is present in most Rab guanosine triphosphatase-activating proteins. TBC1D4 associates with GLUT4-containing membranes under basal conditions and dissociates from membranes with insulin. Here we show that the association of TBC1D4 with membranes is required for its inhibitory action on GLUT4 translocation under basal conditions. Whereas the insulin-dependent dissociation of TBC1D4 from membranes was not required for GLUT4 translocation, its phosphorylation was essential. Many agonists that stimulate GLUT4 translocation failed to trigger TBC1D4 translocation to the cytosol, but in most cases these agonists stimulated TBC1D4 phosphorylation at T642, and their effects on GLUT4 translocation were inhibited by overexpression of the TBC1D4 phosphorylation mutant (TBC1D4-4P). We postulate that TBC1D4 acts to impede GLUT4 translocation by disarming a Rab protein found on GLUT4-containing-membranes and that phosphorylation of TBC1D4 per se is sufficient to overcome this effect, allowing GLUT4 translocation to the cell surface to proceed. Copyright © 2008 by The Endocrine Society. | en_HK |
dc.language | eng | en_HK |
dc.publisher | Endocrine Society. The Journal's web site is located at http://mend.endojournals.org/ | en_HK |
dc.relation.ispartof | Molecular Endocrinology | en_HK |
dc.rights | Molecular Endocrinology. Copyright © The Endocrine Society. | en_HK |
dc.subject.mesh | 3T3-L1 Cells | en_HK |
dc.subject.mesh | Androstadienes - pharmacology | en_HK |
dc.subject.mesh | Animals | en_HK |
dc.subject.mesh | CHO Cells | en_HK |
dc.subject.mesh | Cell Membrane - metabolism - physiology | en_HK |
dc.subject.mesh | Cells, Cultured | en_HK |
dc.subject.mesh | Cricetinae | en_HK |
dc.subject.mesh | Cricetulus | en_HK |
dc.subject.mesh | Cytosol - drug effects - metabolism | en_HK |
dc.subject.mesh | GTPase-Activating Proteins - chemistry - metabolism - physiology | en_HK |
dc.subject.mesh | Glucose Transporter Type 4 - metabolism | en_HK |
dc.subject.mesh | Insulin - pharmacology | en_HK |
dc.subject.mesh | Mice | en_HK |
dc.subject.mesh | Muscle Fibers, Skeletal - drug effects - metabolism - physiology | en_HK |
dc.subject.mesh | Phosphorylation - drug effects - physiology | en_HK |
dc.subject.mesh | Protein Kinase Inhibitors - pharmacology | en_HK |
dc.subject.mesh | Protein Structure, Tertiary - physiology | en_HK |
dc.subject.mesh | Protein Transport - drug effects | en_HK |
dc.subject.mesh | Transport Vesicles - metabolism - physiology | en_HK |
dc.subject.mesh | rab GTP-Binding Proteins - metabolism | en_HK |
dc.title | Regulation of glucose transporter 4 translocation by the rab guanosine triphosphatase-activating protein AS160/TBC1D4: Role of phosphorylation and membrane association | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0888-8809&volume=22&spage=2703&epage=15&date=2008&atitle=Regulation+of+glucose+transporter+4+translocation+by+the+Rab+guanosine+triphosphatase-activating+protein+AS160/TBC1D4:+role+of+phosphorylation+and+membrane+association. | en_HK |
dc.identifier.email | Xu, A:amxu@hkucc.hku.hk | en_HK |
dc.identifier.authority | Xu, A=rp00485 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1210/me.2008-0111 | en_HK |
dc.identifier.pmid | 18801932 | - |
dc.identifier.scopus | eid_2-s2.0-56749173518 | en_HK |
dc.identifier.hkuros | 157973 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-56749173518&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 22 | en_HK |
dc.identifier.issue | 12 | en_HK |
dc.identifier.spage | 2703 | en_HK |
dc.identifier.epage | 2715 | en_HK |
dc.identifier.isi | WOS:000261305200010 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Stöckli, J=17234006800 | en_HK |
dc.identifier.scopusauthorid | Davey, JR=8043218900 | en_HK |
dc.identifier.scopusauthorid | HohnenBehrens, C=15062874400 | en_HK |
dc.identifier.scopusauthorid | Xu, A=7202655409 | en_HK |
dc.identifier.scopusauthorid | James, DE=7401733057 | en_HK |
dc.identifier.scopusauthorid | Ramm, G=7006307479 | en_HK |
dc.identifier.issnl | 0888-8809 | - |