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Gene Review

AP1G1  -  adaptor-related protein complex 1, gamma 1...

Homo sapiens

Synonyms: ADTG, AP-1 complex subunit gamma-1, Adaptor protein complex AP-1 subunit gamma-1, Adaptor-related protein complex 1 subunit gamma-1, CLAPG1, ...
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Disease relevance of AP1G1

  • Because the pattern of androgen metabolism is most probably changed in many cases of hirsutism, these data suggest that for research purposes, it would be preferable to measure 3 beta-diol-G and ADTG in addition to 3 alpha-diol-G in order to gain additional information concerning androgen metabolites in this disorder [1].
  • While preliminary data indicates that both 3 alpha-diolG and androsterone G (ADTG) may arise from adrenal steroid precursors, there have been no reports of C19 steroid glucuronides in women with non-classical, or late-onset congenital adrenal hyperplasia (NC-CAH), who constitute a significant proportion of the hirsute female population [2].

High impact information on AP1G1


Biological context of AP1G1


Anatomical context of AP1G1


Associations of AP1G1 with chemical compounds


Physical interactions of AP1G1


Other interactions of AP1G1

  • Yeast two-hybrid analysis showed that the AGEH domains of the GGA proteins as well as those of gamma-adaptins are able to interact with gamma-synergin, which was previously shown to localized in the TGN region and interact with gamma-adaptin [16].
  • We have identified a human approximately 87-kDa protein, designated as gamma2-adaptin, that is similar to gamma-adaptin (called gamma1-adaptin in this paper), a large chain of the AP-1 clathrin-associated adaptor complex, not only in the primary structure (60% amino acid identity) but also in the domain organization [18].
  • The Golgi-associated, gamma-adaptin homologous, ADP-ribosylation factor (ARF)-interacting proteins (GGAs) are adaptors that sort receptors from the trans-Golgi network into the endosomallysosomal pathway [19].
  • The Golgi-localized, gamma-adaptin ear-containing, ARF-binding (GGA) proteins are monomeric clathrin adaptors that mediate the sorting of cargo at the trans-Golgi network and endosomes [20].
  • Vear, a novel Golgi-associated protein with VHS and gamma-adaptin "ear" domains [11].

Analytical, diagnostic and therapeutic context of AP1G1

  • Northern blot analysis of the mouse and human gamma-adaptin genes revealed a ubiquitous and abundant expression, except in human adult lung [6].


  1. Plasma levels of C-19 steroids and 5 alpha-reduced steroid glucuronides in hyperandrogenic and idiopathic hirsute women. Brochu, M., Bélanger, A., Tremblay, R.R. Fertil. Steril. (1987) [Pubmed]
  2. Plasma levels of C19 steroid glucuronides in pre-menopausal women with non-classical congenital adrenal hyperplasia. Whorwood, C.B., Ueshiba, H., del Blazo, P. J. Steroid Biochem. Mol. Biol. (1992) [Pubmed]
  3. A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome. Hirst, J., Lui, W.W., Bright, N.A., Totty, N., Seaman, M.N., Robinson, M.S. J. Cell Biol. (2000) [Pubmed]
  4. Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin. Page, L.J., Sowerby, P.J., Lui, W.W., Robinson, M.S. J. Cell Biol. (1999) [Pubmed]
  5. In polarized MDCK cells basolateral vesicles arise from clathrin-gamma-adaptin-coated domains on endosomal tubules. Futter, C.E., Gibson, A., Allchin, E.H., Maxwell, S., Ruddock, L.J., Odorizzi, G., Domingo, D., Trowbridge, I.S., Hopkins, C.R. J. Cell Biol. (1998) [Pubmed]
  6. Cloning, expression pattern, and chromosomal assignment to 16q23 of the human gamma-adaptin gene (ADTG). Peyrard, M., Parveneh, S., Lagercrantz, S., Ekman, M., Fransson, I., Sahlén, S., Dumanski, J.P. Genomics (1998) [Pubmed]
  7. Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3. Miller, G.J., Mattera, R., Bonifacino, J.S., Hurley, J.H. Nat. Struct. Biol. (2003) [Pubmed]
  8. Phosphorylation-induced conformational changes regulate GGAs 1 and 3 function at the trans-Golgi network. Ghosh, P., Kornfeld, S. J. Biol. Chem. (2003) [Pubmed]
  9. GGAs: roles of the different domains and comparison with AP-1 and clathrin. Hirst, J., Lindsay, M.R., Robinson, M.S. Mol. Biol. Cell (2001) [Pubmed]
  10. Cytotoxicity of brefeldin A correlates with its inhibitory effect on membrane binding of COP coat proteins. Torii, S., Banno, T., Watanabe, T., Ikehara, Y., Murakami, K., Nakayama, K. J. Biol. Chem. (1995) [Pubmed]
  11. Vear, a novel Golgi-associated protein with VHS and gamma-adaptin "ear" domains. Poussu, A., Lohi, O., Lehto, V.P. J. Biol. Chem. (2000) [Pubmed]
  12. Interactions between adaptor protein-1 of the clathrin coat and microtubules via type 1a microtubule-associated proteins. Orzech, E., Livshits, L., Leyt, J., Okhrimenko, H., Reich, V., Cohen, S., Weiss, A., Melamed-Book, N., Lebendiker, M., Altschuler, Y., Aroeti, B. J. Biol. Chem. (2001) [Pubmed]
  13. 100-kD proteins of Golgi- and trans-Golgi network-associated coated vesicles have related but distinct membrane binding properties. Wong, D.H., Brodsky, F.M. J. Cell Biol. (1992) [Pubmed]
  14. Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/gamma-adaptin vesicles at the trans-Golgi network. Karlsson, K., Carlsson, S.R. J. Biol. Chem. (1998) [Pubmed]
  15. The GRIP domain is a specific targeting sequence for a population of trans-Golgi network derived tubulo-vesicular carriers. Brown, D.L., Heimann, K., Lock, J., Kjer-Nielsen, L., van Vliet, C., Stow, J.L., Gleeson, P.A. Traffic (2001) [Pubmed]
  16. Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin. Takatsu, H., Yoshino, K., Nakayama, K. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  17. Gamma-adaptin interacts directly with Rabaptin-5 through its ear domain. Shiba, Y., Takatsu, H., Shin, H.W., Nakayama, K. J. Biochem. (2002) [Pubmed]
  18. Identification and characterization of novel clathrin adaptor-related proteins. Takatsu, H., Sakurai, M., Shin, H.W., Murakami, K., Nakayama, K. J. Biol. Chem. (1998) [Pubmed]
  19. Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor. Suer, S., Misra, S., Saidi, L.F., Hurley, J.H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  20. The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites. Mattera, R., Puertollano, R., Smith, W.J., Bonifacino, J.S. J. Biol. Chem. (2004) [Pubmed]
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