80K-H acts as a signaling bridge in intact living cells between PKCzeta and the GLUT4 translocation regulator Munc18c
80K-H acts as a signaling bridge in intact living cells between PKCzeta and the GLUT4 translocation regulator Munc18c
Insulin triggers the translocation of glucose transporter GLUT4 to the plasma membrane. To understand the nature of the missing links between upstream insulin activated kinases and proteins of the GLUT4 translocation apparatus, the role of 80K-H was examined to test if it was one such missing link in live cells. Fluorescence correlation spectroscopy showed that the mobility of 80K-H was significantly decreased by insulin stimulation. This was dependent on the presence of PKCzeta and an intact binding site for PKCzeta. Insulin also increased the mobility of munc18c in an 80K-H- and PKCzeta dependent manner. These results indicate that insulin induces dynamic associations between PKCzeta, 80K-H, and munc18c and that 80K-H may act as a key signaling link between PKCzeta and munc18c in live cells.
581-589
Smithers, Natalie P.
63ead01b-6515-4f82-a963-884f572af872
Hodgkinson, Conrad P.
292cc7c3-b378-4911-8353-9a8c08a1c737
Cuttle, Mark
018504ba-b5f5-426c-9321-0a0f6bc6e8ef
Sale, Graham J.
81048025-7d8f-4218-969a-bf95ebf50b51
November 2008
Smithers, Natalie P.
63ead01b-6515-4f82-a963-884f572af872
Hodgkinson, Conrad P.
292cc7c3-b378-4911-8353-9a8c08a1c737
Cuttle, Mark
018504ba-b5f5-426c-9321-0a0f6bc6e8ef
Sale, Graham J.
81048025-7d8f-4218-969a-bf95ebf50b51
Smithers, Natalie P., Hodgkinson, Conrad P., Cuttle, Mark and Sale, Graham J.
(2008)
80K-H acts as a signaling bridge in intact living cells between PKCzeta and the GLUT4 translocation regulator Munc18c.
Journal of Receptors and Signal Transduction, 28 (6), .
(doi:10.1080/10799890802598571).
(PMID:19061073)
Abstract
Insulin triggers the translocation of glucose transporter GLUT4 to the plasma membrane. To understand the nature of the missing links between upstream insulin activated kinases and proteins of the GLUT4 translocation apparatus, the role of 80K-H was examined to test if it was one such missing link in live cells. Fluorescence correlation spectroscopy showed that the mobility of 80K-H was significantly decreased by insulin stimulation. This was dependent on the presence of PKCzeta and an intact binding site for PKCzeta. Insulin also increased the mobility of munc18c in an 80K-H- and PKCzeta dependent manner. These results indicate that insulin induces dynamic associations between PKCzeta, 80K-H, and munc18c and that 80K-H may act as a key signaling link between PKCzeta and munc18c in live cells.
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Published date: November 2008
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Local EPrints ID: 160173
URI: http://eprints.soton.ac.uk/id/eprint/160173
ISSN: 1079-9893
PURE UUID: 10676f7e-170c-4b73-a1fc-a777cc363da3
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Date deposited: 12 Jul 2010 10:25
Last modified: 14 Mar 2024 01:56
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Author:
Natalie P. Smithers
Author:
Conrad P. Hodgkinson
Author:
Mark Cuttle
Author:
Graham J. Sale
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