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A potential link between insulin signaling and GLUT4 translocation: Association of Rab10-GTP with the exocyst subunit Exoc6/6b

Sano, Hiroyuki, Peck, Grantley R., Blachon, Stephanie, Lienhard, Gustav E.·2015·Biochemical and Biophysical Research Communications
DOI 10.1016/j.bbrc.2015.08.069PMC PMC4564306
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  • GTP-bound RAB10 mediates insulin-stimulated transport of GLUT4-containing vesicles to the plasma membrane via recruitment of the exocyst membrane tethering complex.

    “Intriguingly, GTP-bound RAB10 has previously been demonstrated to mediate the insulin-stimulated transport of GLUT4-containing vesicles to the plasma membrane via its recruitment of the exocyst membrane tethering complex (44).”

    From The small GTPase RAB10 regulates endosomal recycling of the LDL receptor and transferrin receptor in hepatocytes (2022) · cites this paper as [44]

    The Introduction reports that Rab10-GTP binds the exocyst subunits Exoc6/6b and that these subunits participate in GLUT4 translocation in adipocytes. The Discussion calls this interaction a proposed link to vesicle exocytosis and says how the exocyst interacts with GLUT4 vesicles in response to insulin remains to be determined. Thus, the paper does not demonstrate the claimed recruitment mechanism for transport to the plasma membrane. (LLM, conf=0.87)

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Research works printed but not linked: 29

  1. Leto, 2012, Regulation of glucose transport by insulin: traffic control of GLUT4, Nat. Rev. Mol. Cell Biol., 13, 383, 10.1038/nrm3351 · DOI · Paper page
  2. Klip, 2014, Signal transduction meets vesicle traffic: the software and hardware of GLUT4 translocation, Am. J. Physiol. Cell Physiol., 306, C879, 10.1152/ajpcell.00069.2014 · DOI
  3. Sakamoto, 2008, Emerging role for As160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic, Am. J. Physiol. Endocrinol. Metab., 295, E29, 10.1152/ajpendo.90331.2008 · DOI · Paper page
  4. Sano, 2011, Insulin-stimulated GLUT4 translocation in adipocytes requires the Rab10 guanine nucleotide exchange factor Dennd4C, J. Biol. Chem., 286, 16541, 10.1074/jbc.C111.228908 · DOI
  5. Chen, 2012, Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes, J. Cell. Biol., 198, 545, 10.1083/jcb.201111091 · DOI
  6. Sadacca, 2013, Specialized sorting of GLUT4 and its recruitment to the cell surface are independently regulated by distinct rabs, Mol. Biol. Cell, 24, 2544, 10.1091/mbc.e13-02-0103 · DOI
  7. Karunanithi, 2014, A Rab10:RalA G protein cascade regulates insulin-stimulated glucose uptake in adipocytes, Mol. Biol. Cell, 25, 3059, 10.1091/mbc.e14-06-1060 · DOI
  8. He, 2009, The exocyst complex in polarized exocytosis, Curr. Opin. Cell Biol., 21, 537, 10.1016/j.ceb.2009.04.007 · DOI · Paper page
  9. Heider, 2012, Exorcising the exocyst complex, Traffic, 13, 898, 10.1111/j.1600-0854.2012.01353.x · DOI
  10. Luo, 2014, The role of Sec3p in secretory vesicle targeting and exocyst complex assembly, Mol. Cell Biol., 25, 3813, 10.1091/mbc.e14-04-0907 · DOI
  11. Rivera-Molina, 2013, Live-cell imaging of the exocyst links its spatiotemporal dynamics to various stages of vesicle fusion, J. Cell Biol., 201, 673, 10.1083/jcb.201212103 · DOI
  12. Inoue, 2003, The exocyst complex is required for targeting of GLUT4 to the plasma membrane by insulin, Nature, 422, 629, 10.1038/nature01533 · DOI
  13. Inoue, 2006, Compartmentalization of the exocyst complex in lipid rafts controls GLUT4 vesicle tethering, Mol. Biol. Cell, 17, 2303, 10.1091/mbc.e06-01-0030 · DOI
  14. Ewart, 2005, Evidence for a role of the exocyst in insulin-stimulated Glut4 trafficking in 3T3-L1 adipocytes, J. Biol. Chem., 280, 3812, 10.1074/jbc.M409928200 · DOI
  15. Brymora, 2001, The brain exocyst complex interacts with RalA in a GTP-dependent manner, J. Biol. Chem., 276, 29792, 10.1074/jbc.C100320200 · DOI · Paper page
  16. Zhang, 2004, Sec15 is an effector for the Rab11 GTPase in mammalian cells, J. Biol. Chem., 279, 43027, 10.1074/jbc.M402264200 · DOI · Paper page
  17. Lim, 2005, A mutation in Sec15l1 causes anemia in hemoglobin deficit (hbd) mice, Nat. Genet., 37, 1270, 10.1038/ng1659 · DOI
  18. Chavez, 2008, Inhibition of GLUT4 translocation by Tbc1d1, a Rab GTPase-activating protein abundant in skeletal muscle, is partially relieved by AMP-activated protein kinase activation, J. Biol. Chem., 238, 9187, 10.1074/jbc.M708934200 · DOI
  19. Sano, 2007, Rab10, a target of the AS160 GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane, Cell Metab., 5, 293, 10.1016/j.cmet.2007.03.001 · DOI · Paper page
  20. Sano, 2008, Rab10 in insulin-stimulated GLUT4 translocation, Biochem. J., 411, 89, 10.1042/BJ20071318 · DOI
  21. Fromont-Racine, 1997, Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens, Nat. Genet., 16, 277, 10.1038/ng0797-277 · DOI
  22. Shi, 2010, EHBP-1 functions with RAB-10 during endocytic recycling in caenorhabditis elegans, Mol. Biol. Cell, 21, 2930, 10.1091/mbc.e10-02-0149 · DOI
  23. Fukuda, 2008, Large scale screening for novel rab effectors reveals unexpected broad rab binding specificity, Mol. Cell. Proteomics, 7, 1031, 10.1074/mcp.M700569-MCP200 · DOI
  24. Roland, 2009, Alternative splicing in class V myosins determines association with Rab10, J. Biol. Chem., 284, 1213, 10.1074/jbc.M805957200 · DOI · Paper page
  25. Vitale, 1998, Distinct rab-binding domains mediate the interaction of rabaptin-5 with GTP-bound Rab4 and Rab5, EMBO J., 17, 1941, 10.1093/emboj/17.7.1941 · DOI
  26. Wu, 2005, Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo, Nat. Struct. Mol. Biol., 12, 879, 10.1038/nsmb987 · DOI
  27. Lee, 2009, Structural mechanisms for regulation of membrane traffic by Rab GTPases, Traffic, 10, 1377, 10.1111/j.1600-0854.2009.00942.x · DOI
  28. Babbey, 2010, Rab10 associates with primary cilia and the exocyst complex in renal epithelial cells, Am. J. Physiol. Ren. Physiol., 299, F495, 10.1152/ajprenal.00198.2010 · DOI · Paper page
  29. Boyd, 2004, Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p, J. Cell Biol., 167, 889, 10.1083/jcb.200408124 · DOI · Paper page

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Metadata

Authors
Sano, H., Peck, G. R., Blachon, S., & Lienhard, G. E.
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2015-09
Volume
465
Issue
3
Pages
601-605
ISSN
0006-291X
DOI
10.1016/j.bbrc.2015.08.069
PMC
PMC4564306
Cited by
35
References
0
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Funders
NIH (DK025336)

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