Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.18/171
Título: Protein kinase WNK1 promotes cell surface expression of glucose transporter GLUT1 by regulating a Tre-2/USP6-BUB2-Cdc16 domain family member 4 (TBC1D4)-Rab8A complex
Autor: Mendes, Ana Isabel
Matos, Paulo
Moniz, Sónia
Jordan, Peter
Palavras-chave: Vias de Transdução de Sinal e Patologias Associadas
Data: 10-Dez-2010
Editora: American Society for Biochemistry and Molecular Biology
Citação: J Biol Chem. 2010 Dec 10;285(50):39117-26. Epub 2010 Oct 11
Resumo: One mechanism by which mammalian cells regulate the uptake of glucose is the number of glucose transporter proteins (GLUT) present at the plasma membrane. In insulin-responsive cells types, GLUT4 is released from intracellular stores through inactivation of the Rab GTPase activating protein Tre-2/USP6-BUB2-Cdc16 domain family member 4 (TBC1D4) (also known as AS160). Here we describe that TBC1D4 forms a protein complex with protein kinase WNK1 in human embryonic kidney (HEK293) cells. We show that WNK1 phosphorylates TBC1D4 in vitro and that the expression levels of WNK1 in these cells regulate surface expression of the constitutive glucose transporter GLUT1. WNK1 was found to increase the binding of TBC1D4 to regulatory 14-3-3 proteins while reducing its interaction with the exocytic small GTPase Rab8A. These effects were dependent on the catalytic activity because expression of a kinase-dead WNK1 mutant had no effect on binding of 14-3-3 and Rab8A, or on surface GLUT1 levels. Together, the data describe a pathway regulating constitutive glucose uptake via GLUT1, the expression level of which is related to several human diseases.
Peer review: yes
URI: http://hdl.handle.net/10400.18/171
ISSN: 0021-9258
Versão do Editor: http://www.jbc.org/content/285/50/39117.abstract
Aparece nas colecções:DGH - Artigos em revistas internacionais

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