TBC1D4

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TBC1 domain family, member 4
Identifiers
Symbols TBC1D4 ; AS160; DKFZp779C0666
External IDs Template:MGI HomoloGene: 45451
RNA expression pattern
File:PBB GE TBC1D4 203386 at tn.png
File:PBB GE TBC1D4 203387 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

TBC1 domain family, member 4, also known as TBC1D4 and AS160, is a human gene.[1]

The 160 kD protein product was first discovered in a screen for novel substrates of the serine-threonine kinase Akt, which phosphorylates AS160 after insulin stimulation.[2] Insulin stimulation of fat and muscle cells results in translocation of the glucose transporter GLUT4 to the plasma membrane, and this translocation process is dependent on phosphorylation of AS160.[3] The role of AS160 in GLUT4 translocation is mediated by its GTPase activating domain, which interacts with Rab proteins in vesicle formation. Specifically, AS160 activates RAB2A, RAB8A, RAB10 and RAB14.[4]

AS160 also contains a calmodulin-binding domain, and this domain mediates phosphorylation-independent glucose uptake in muscle cells.[5]


References

  1. ↑ "Entrez Gene: TBC1D4 TBC1 domain family, member 4".
  2. ↑ Kane S, Sano H, Liu SC; et al. (2002). "A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain". J. Biol. Chem. 277 (25): 22115–8. doi:10.1074/jbc.C200198200. PMID 11994271.
  3. ↑ Sano H, Kane S, Sano E; et al. (2003). "Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation". J. Biol. Chem. 278 (17): 14599–602. doi:10.1074/jbc.C300063200. PMID 12637568.
  4. ↑ Mîinea CP, Sano H, Kane S; et al. (2005). "AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain". Biochem. J. 391 (Pt 1): 87–93. doi:10.1042/BJ20050887. PMID 15971998.
  5. ↑ Kramer HF, Taylor EB, Witczak CA, Fujii N, Hirshman MF, Goodyear LJ (2007). "Calmodulin-binding domain of AS160 regulates contraction- but not insulin-stimulated glucose uptake in skeletal muscle". Diabetes. 56 (12): 2854–62. doi:10.2337/db07-0681. PMID 17717281.

Further reading

  • Nagase T, Ishikawa K, Miyajima N; et al. (1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (1): 31–9. PMID 9628581.
  • Kurihara LJ, Semenova E, Miller W; et al. (2002). "Candidate genes required for embryonic development: a comparative analysis of distal mouse chromosome 14 and human chromosome 13q22". Genomics. 79 (2): 154–61. doi:10.1006/geno.2002.6692. PMID 11829485.
  • Nakayama M, Kikuno R, Ohara O (2003). "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs". Genome Res. 12 (11): 1773–84. doi:10.1101/gr.406902. PMID 12421765.
  • Lee SY, Obata Y, Yoshida M; et al. (2003). "Immunomic analysis of human sarcoma". Proc. Natl. Acad. Sci. U.S.A. 100 (5): 2651–6. doi:10.1073/pnas.0437972100. PMID 12601173.
  • Dunham A, Matthews LH, Burton J; et al. (2004). "The DNA sequence and analysis of human chromosome 13". Nature. 428 (6982): 522–8. doi:10.1038/nature02379. PMID 15057823.
  • Beausoleil SA, Jedrychowski M, Schwartz D; et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.
  • Matsumoto Y, Imai Y, Lu Yoshida N; et al. (2004). "Upregulation of the transcript level of GTPase activating protein KIAA0603 in T cells from patients with atopic dermatitis". FEBS Lett. 572 (1–3): 135–40. doi:10.1016/j.febslet.2004.07.023. PMID 15304337.
  • Jin J, Smith FD, Stark C; et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
  • Karlsson HK, Zierath JR, Kane S; et al. (2005). "Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects". Diabetes. 54 (6): 1692–7. PMID 15919790.
  • Kim JE, Tannenbaum SR, White FM (2005). "Global phosphoproteome of HT-29 human colon adenocarcinoma cells". J. Proteome Res. 4 (4): 1339–46. doi:10.1021/pr050048h. PMID 16083285.
  • Beausoleil SA, Villén J, Gerber SA; et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
  • Treebak JT, Birk JB, Rose AJ; et al. (2007). "AS160 phosphorylation is associated with activation of alpha2beta2gamma1- but not alpha2beta2gamma3-AMPK trimeric complex in skeletal muscle during exercise in humans". Am. J. Physiol. Endocrinol. Metab. 292 (3): E715–22. doi:10.1152/ajpendo.00380.2006. PMID 17077344.
  • Olsen JV, Blagoev B, Gnad F; et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
  • Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.
  • Howlett KF, Sakamoto K, Garnham A; et al. (2007). "Resistance exercise and insulin regulate AS160 and interaction with 14-3-3 in human skeletal muscle". Diabetes. 56 (6): 1608–14. doi:10.2337/db06-1398. PMID 17369524.
  • Frøsig C, Rose AJ, Treebak JT; et al. (2007). "Effects of endurance exercise training on insulin signaling in human skeletal muscle: interactions at the level of phosphatidylinositol 3-kinase, Akt, and AS160". Diabetes. 56 (8): 2093–102. doi:10.2337/db06-1698. PMID 17513702.

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