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Daxx functions as a scaffold of a protein assembly constituted by GLUT4, JNK1 and KIF5B
Author(s) -
Lalioti Vasiliki S.,
Vergarajauregui Silvia,
Tsuchiya Yo,
HernandezTiedra Sonia,
Sandoval Ignacio V.
Publication year - 2009
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.21614
Subject(s) - glut4 , kinesin , death associated protein 6 , scaffold protein , microbiology and biotechnology , kinase , signal transducing adaptor protein , phosphorylation , glucose transporter , chemistry , biology , biochemistry , transcription factor , nuclear protein , signal transduction , endocrinology , insulin , gene , microtubule
We have previously reported the physical interaction between Daxx, the adaptor protein that mediates activation of the Jun amino‐terminal kinase (JNK), and GLUT4, the insulin‐dependent glucose transporter, interaction that involves their C‐domains. Co‐immunoprecipitation and two‐hybrid‐based protein–protein interaction studies show now that Daxx and GLUT4 interact with JNK1 through D‐sites in their NH 2 ‐(aa 1‐501) and large endofacial loop, respectively. Serum deprivation strongly enhances the association of JNK1 with Daxx and dissociates the kinase from GLUT4. SP600125, a potent JNK1 inhibitor, reduces the JNK1 activity associated with GLUT4 and the phosphorylation of two minor GLUT4 species in serum‐starved 3T3‐L1 adipocytes. In addition, Daxx interacts with kinesin KIF5B through the 6xTPR domain of the kinesin light chain, a domain engaged in the grab hold of protein cargo by kinesin motors that codistribute with JNK. Depletion of Daxx in 3T3‐L1 adipocytes provokes the partial translocation of the GLUT4 retained in the GLUT4 storage compartment to endosomes. J. Cell. Physiol. 218: 416–426, 2009. © 2008 Wiley‐Liss, Inc.