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Adaptor-related protein complex 1, gamma 2 subunit

Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. The adaptin family of proteins is compsed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote the formation of clathrin-coated pits and vesicles. The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. This protein along with the complex is thought to function at some trafficking step in the complex pathways between the trans-Golgi network and the cell surface. There are two alternatively spliced transcript variants of this gene encoding the same protein. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: gamma-adaptin, Ubiquitin, Nedd4, AP1S1, Inactive
Papers on gamma2-adaptin
γ2-Adaptin is functioning in the late endosomal sorting pathway and interacts with ESCRT-I and -III subunits.
Prange et al., Mainz, Germany. In Biochim Biophys Acta, 2010
Data show that gamma2-adaptin in MVB sorting specifically interacts with the ESCRT subunits Vps28 and CHMP2A.
The tumor-associated antigen EBAG9 negatively regulates the cytolytic capacity of mouse CD8+ T cells.
Rehm et al., Berlin, Germany. In J Clin Invest, 2009
We further found that EBAG9 interacts with the adaptor molecule gamma2-adaptin, suggesting EBAG9 is involved in endosomal-lysosomal biogenesis and membrane fusion.
gamma2-Adaptin, a ubiquitin-interacting adaptor, is a substrate to coupled ubiquitination by the ubiquitin ligase Nedd4 and functions in the endosomal pathway.
Prange et al., Mainz, Germany. In J Biol Chem, 2008
gamma2-adaptin's ubiquitin-interacting motif mediates a specific physical interaction with the ubiquitin ligase Nedd4 and promotes ubiquitination of gamma2-adaptin
Hepatitis B virus maturation is sensitive to functional inhibition of ESCRT-III, Vps4, and gamma 2-adaptin.
Prange et al., Mainz, Germany. In J Virol, 2007
These results demonstrate that HBV exploits the multivesicular bodies machinery with the aid of gamma 2-adaptin.
Gamma-adaptin, a novel ubiquitin-interacting adaptor, and Nedd4 ubiquitin ligase control hepatitis B virus maturation.
Prange et al., Mainz, Germany. In J Biol Chem, 2006
Here we report that HBV uses cellular gamma2-adaptin and Nedd4, possibly in conjunction with ubiquitin, to coordinate its assembly and release.
Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex.
Bonifacino et al., Bethesda, United States. In Embo J, 2003
These interactions are bipartite: GGA-GAE domains recognize an FGPLV sequence (residues 439-443) in a predicted random coil of Rabaptin-5 (a sequence also recognized by the gamma1- and gamma2-adaptin ears), while GGA-GAT domains bind to the C-terminal coiled-coils of Rabaptin-5.
Hepatitis B virus large envelope protein interacts with gamma2-adaptin, a clathrin adaptor-related protein.
Prange et al., Mainz, Germany. In J Virol, 2001
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.
Identification and characterization of novel clathrin adaptor-related proteins.
Nakayama et al., Tsukuba, Japan. In J Biol Chem, 1998
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.
Cloning, expression, and localization of a novel gamma-adaptin-like molecule.
Mellman et al., New Haven, United States. In Febs Lett, 1998
We describe the cloning, expression, and localization of gamma2-adaptin, a novel isoform of gamma-adaptin.
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