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Gene Review

AP1G2  -  adaptor-related protein complex 1, gamma 2...

Homo sapiens

Synonyms: AP-1 complex subunit gamma-like 2, G2AD, G2ad, Gamma2-adaptin
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Disease relevance of AP1G2


High impact information on AP1G2

  • 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 [2].
  • Furthermore, unlike gamma1-adaptin, gamma2-adaptin is recruited onto membranes in the presence of a fungal antibiotic, brefeldin A [2].
  • Together, the results suggest a role for gamma2-adaptin in L-mediated processes of viral biogenesis and/or pathogenesis, such as facilitating and guiding HBV assembly [1].
  • With this approach, we have identified gamma2-adaptin, a putative member of the clathrin adaptor proteins responsible for protein sorting and trafficking, as a specific binding partner of L protein [1].
  • Evidence for a physical interaction between L protein and gamma2-adaptin was also demonstrated by affinity chromatography and coimmunoprecipitation, and the binding sites were mapped to the L-specific pre-S1 domain and the gamma2-adaptin-specific ear domain [1].

Anatomical context of AP1G2

  • Analysis of an L mutant protein indicates that the L-gamma2-adaptin interaction strictly depends on the pre-S1 domain of transmembrane L protein oriented to the cytosol and thus appears to occur in the cytosolic environment [1].

Associations of AP1G2 with chemical compounds

  • The membrane association of gamma- and gamma2-adaptin could further be distinguished by differential sensitivity to the fungal metabolite brefeldin A, gamma2-adaptin binding being insensitive to drug treatment [3].

Regulatory relationships of AP1G2

  • Excess gamma 2-adaptin blocked HBV production in a manner similar to the actions of CHMP and Vps4 mutants [4].

Analytical, diagnostic and therapeutic context of AP1G2

  • Immunofluorescence microscopy analysis has revealed that gamma2-adaptin is localized to paranuclear vesicular structures that are not superimposed on structures containing gamma1-adaptin [2].


  1. Hepatitis B virus large envelope protein interacts with gamma2-adaptin, a clathrin adaptor-related protein. Hartmann-Stühler, C., Prange, R. J. Virol. (2001) [Pubmed]
  2. 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]
  3. Cloning, expression, and localization of a novel gamma-adaptin-like molecule. Lewin, D.A., Sheff, D., Ooi, C.E., Whitney, J.A., Yamamoto, E., Chicione, L.M., Webster, P., Bonifacino, J.S., Mellman, I. FEBS Lett. (1998) [Pubmed]
  4. Hepatitis B virus maturation is sensitive to functional inhibition of ESCRT-III, Vps4, and gamma 2-adaptin. Lambert, C., Döring, T., Prange, R. J. Virol. (2007) [Pubmed]
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