You are not logged in.

Interaction of the Akt substrate, AS160, with the glucose transporter 4 vesicle marker protein, insulin-regulated aminopeptidase

Peck, Grantley R., Ye, Siying, Pham, Vi, Fernando, Ruani N., Macaulay, S. Lance, Chai, Siew Yeen and Albiston, Anthony L. 2006, Interaction of the Akt substrate, AS160, with the glucose transporter 4 vesicle marker protein, insulin-regulated aminopeptidase, Molecular endocrinology, vol. 20, no. 10, pp. 2576-2583, doi: 10.1210/me.2005-0476.

Attached Files
Name Description MIMEType Size Downloads

Title Interaction of the Akt substrate, AS160, with the glucose transporter 4 vesicle marker protein, insulin-regulated aminopeptidase
Author(s) Peck, Grantley R.
Ye, Siying
Pham, Vi
Fernando, Ruani N.
Macaulay, S. Lance
Chai, Siew Yeen
Albiston, Anthony L.
Journal name Molecular endocrinology
Volume number 20
Issue number 10
Start page 2576
End page 2583
Publisher Endocrine Society
Place of publication Chevy Chase, Md.
Publication date 2006-10
ISSN 0888-8809
1944-9917
Summary Insulin-regulated aminopeptidase (IRAP), a marker of glucose transporter 4 (GLUT4) storage vesicles (GSVs), is the only protein known to traffic with GLUT4. In the basal state, GSVs are sequestered from the constitutively recycling endosomal system to an insulin-responsive, intracellular pool. Insulin induces a rapid translocation of GSVs to the cell surface from this pool, resulting in the incorporation of IRAP and GLUT4 into the plasma membrane. We sought to identify proteins that interact with IRAP to further understand this GSV trafficking process. This study describes our identification of a novel interaction between the amino terminus of IRAP and the Akt substrate, AS160 (Akt substrate of 160 kDa). The validity of this interaction was confirmed by coimmunoprecipitation of both overexpressed and endogenous proteins. Moreover, confocal microscopy demonstrated colocalization of these proteins. In addition, we demonstrate that the IRAP-binding domain of AS160 falls within its second phosphotyrosine-binding domain and the interaction is not regulated by AS160 phosphorylation. We hypothesize that AS160 is localized to GLUT4-containing vesicles via its interaction with IRAP where it inhibits the activity of Rab substrates in its vicinity, effectively tethering the vesicles intracellularly.
Language eng
DOI 10.1210/me.2005-0476
Field of Research 119999 Medical and Health Sciences not elsewhere classified
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2006, The Endocrine Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30040948

Document type: Journal Article
Collection: School of Medicine
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 60 times in TR Web of Science
Scopus Citation Count Cited 63 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 178 Abstract Views, 3 File Downloads  -  Detailed Statistics
Created: Wed, 07 Dec 2011, 10:05:04 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.