Skip to main content
SpringerLink
Log in

AGAP1

  • Living reference work entry
  • First Online:
Encyclopedia of Signaling Molecules

  • 90 Accesses

Synonyms

AGAP-1; Arf GAP with GTP-binding protein-like, ANK repeat and PH; ArfGAP with GTPase domain, ankyrin repeat, and PH domain 1; Centaurin, gamma 2; Centaurin-gamma-2; CENTG2; Cnt-G2; GGAP1; GTP-binding and GTPase-activating protein 1; KIAA1099

Historical Background

The ADP-ribosylation factor (ARF) family of small GTP-binding proteins are ubiquitously expressed and involved in many cellular events such as cell adhesion, cell migration, neurite outgrowth, cell secretion, and endocytosis (D’Souza-Schorey and Chavrier 2006). In mammals, the ARF family consists of six members (ARFs 1–6), and ARFs 1–5 function at the Golgi whereas ARF6 regulates cellular events at the plasma membrane (Donaldson and Jackson 2011). Since ARFs belong to the Ras superfamily of GTPases, they act as molecular switches by cycling between inactive GDP-bound and active GTP-bound forms. They depend on guanine exchange factors (GEFs) for activation and GTPase-activating proteins (GAPs) for inactivation...

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution

Institutional subscriptions

References

  • Bendor J, Lizardi-Ortiz JE, Westphalen RI, Brandstetter M, Hemmings Jr HC, Sulzer D, et al. AGAP1/AP-3-dependent endocytic recycling of M5 muscarinic receptors promotes dopamine release. EMBO J. 2010;29:2813–26. doi:10.1038/emboj.2010.154.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • D’Souza-Schorey C, Chavrier P. ARF proteins: roles in membrane traffic and beyond. Nat Rev Mol Cell Biol. 2006;7:347–58.

    Article  PubMed  Google Scholar 

  • Donaldson JG, Honda A. Localization and function of Arf family GTPases. Biochem Soc Trans. 2005;33:639–42. doi:10.1042/bst0330639.

    Article  CAS  PubMed  Google Scholar 

  • Donaldson JG, Jackson CL. ARF family G proteins and their regulators: roles in membrane transport, development and disease. Nat Rev Mol Cell Biol. 2011;12:362–75. doi:10.1038/nrm3117.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Gan TQ, Tang RX, He RQ, Dang YW, Xie Y, Chen G. Upregulated MiR-1269 in hepatocellular carcinoma and its clinical significance. Int J Clin Exp Med. 2015;8:714–21.

    CAS  PubMed  PubMed Central  Google Scholar 

  • Harvey RC, Mullighan CG, Wang X, Dobbin KK, Davidson GS, Bedrick EJ, et al. Identification of novel cluster groups in pediatric high-risk B-precursor acute lymphoblastic leukemia with gene expression profiling: correlation with genome-wide DNA copy number alterations, clinical characteristics, and outcome. Blood. 2010;116:4874–84. doi:10.1182/blood-2009-08-239681.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Hirokawa N, Noda Y, Tanaka Y, Niwa S. Kinesin superfamily motor proteins and intracellular transport. Nat Rev Mol Cell Biol. 2009;10:682–96. doi:10.1038/nrm2774.

    Article  CAS  PubMed  Google Scholar 

  • Jaffe AB, Hall A. Rho GTPases: biochemistry and biology. Annu Rev Cell Dev Biol. 2005;21:247–69. doi:10.1146/annurev.cellbio.21.020604.150721.

    Article  CAS  PubMed  Google Scholar 

  • Kahn RA, Bruford E, Inoue H, Logsdon Jr JM, Nie Z, Premont RT, et al. Consensus nomenclature for the human ArfGAP domain-containing proteins. J Cell Biol. 2008;182:1039–44. doi:10.1083/jcb.200806041.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Luo R, Akpan IO, Hayashi R, Sramko M, Barr V, Shiba Y, et al. GTP-binding protein-like domain of AGAP1 is protein binding site that allosterically regulates ArfGAP protein catalytic activity. J Biol Chem. 2012;287:17176–85. doi:10.1074/jbc.M111.334458.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Luo R, Chen PW, Wagenbach M, Jian X, Jenkins L, Wordeman L, et al. Direct functional interaction of the kinesin-13 family membrane kinesin like protein 2A (Kif2A) and Arf GAP with GTP-binding protein-like, ankyrin repeats and PH domains1 (AGAP1). J Biol Chem. 2016. doi:10.1074/jbc.M116.732479.

    Google Scholar 

  • McMichael G, Bainbridge MN, Haan E, Corbett M, Gardner A, Thompson S, et al. Whole-exome sequencing points to considerable genetic heterogeneity of cerebral palsy. Mol Psychiatry. 2015;20:176–82. doi:10.1038/mp.2014.189.

    Article  CAS  PubMed  Google Scholar 

  • Meurer S, Pioch S, Wagner K, Muller-Esterl W, Gross S. AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl cyclase. J Biol Chem. 2004;279:49346–54. doi:10.1074/jbc.M410565200.

    Article  CAS  PubMed  Google Scholar 

  • Nie Z, Stanley KT, Stauffer S, Jacques KM, Hirsch DS, Takei J, et al. AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton. J Biol Chem. 2002;277:48965–75. doi:10.1074/jbc.M202969200.

    Article  CAS  PubMed  Google Scholar 

  • Nie Z, Boehm M, Boja ES, Vass WC, Bonifacino JS, Fales HM, et al. Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1. Dev Cell. 2003;5:513–21.

    Article  CAS  PubMed  Google Scholar 

  • Nie Z, Fei J, Premont RT, Randazzo PA. The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3. J Cell Sci. 2005;118:3555–66. doi:10.1242/jcs.02486.

    Article  CAS  PubMed  Google Scholar 

  • Robinson MS, Bonifacino JS. Adaptor-related proteins. Curr Opin Cell Biol. 2001;13:444–53.

    Article  CAS  PubMed  Google Scholar 

  • Saraste M, Hyvonen M. Pleckstrin homology domains: a fact file. Curr Opin Struct Biol. 1995;5:403–8.

    Article  CAS  PubMed  Google Scholar 

  • Steffan JJ, Snider JL, Skalli O, Welbourne T, Cardelli JA. Na+/H+ exchangers and RhoA regulate acidic extracellular pH-induced lysosome trafficking in prostate cancer cells. Traffic. 2009;10:737–53. doi:10.1111/j.1600-0854.2009.00904.x.

    Article  CAS  PubMed  Google Scholar 

  • Wassink TH, Piven J, Vieland VJ, Jenkins L, Frantz R, Bartlett CW, et al. Evaluation of the chromosome 2q37.3 gene CENTG2 as an autism susceptibility gene. Am J Med Genet B Neuropsychiatr Genet. 2005;136B:36–44. doi:10.1002/ajmg.b.30180.

    Article  PubMed  Google Scholar 

  • Yan J, Wen W, Xu W, Long J-f, Adams ME, Froehner SC, et al. Structure of the split PH domain and distinct lipid-binding properties of the PH–PDZ supramodule of α-syntrophin. EMBO J. 2005;24:3985–95. doi:10.1038/sj.emboj.7600858.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Life Science 1, School of Medicine, Swansea University, Singleton Park, Swansea, SA2 8PP, Wales, UK

    Salman Tamaddon-Jahromi & Venkateswarlu Kanamarlapudi

Authors
  1. Salman Tamaddon-Jahromi
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Venkateswarlu Kanamarlapudi
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Venkateswarlu Kanamarlapudi .

Editor information

Editors and Affiliations

  1. Dept. Biological Science, Department of Molecular Science and Tech College of Natural Science, Suwon, Korea (Republic of)

    Sangdun Choi

Rights and permissions

Reprints and permissions

Copyright information

© 2016 Crown Copyright

About this entry

Cite this entry

Tamaddon-Jahromi, S., Kanamarlapudi, V. (2016). AGAP1. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_101963-1

Download citation

  • DOI: https://doi.org/10.1007/978-1-4614-6438-9_101963-1

  • Received:

  • Accepted:

  • Published:

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4614-6438-9

  • Online ISBN: 978-1-4614-6438-9

  • eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences

Publish with us

Policies and ethics

Search

Navigation