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SYNRG  -  synergin, gamma

Homo sapiens

Synonyms: AP1 subunit gamma-binding protein 1, AP1GBP1, Gamma-synergin, MGC104959, SYNG, ...
 
 
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High impact information on AP1GBP1

  • In cells expressing alpha-adaptin with the gamma-adaptin ear, a construct that goes mainly to the plasma membrane, much of the gamma-synergin is also rerouted to the plasma membrane, indicating that it follows AP-1 onto membranes rather than leading it there [1].
  • The gamma 1-adaptin subunits of AP-1 and GGA possess homologous ear domains involved in the recruitment of accessory proteins, gamma-synergin and Rabaptin-5 [2].
  • By gel filtration, aftiphilin coelutes with two other AP-1 binding partners, p200a and gamma-synergin [3].
  • By overexpressing wild-type GGA and gamma appendage domains in cells, we can drive p56 and gamma-synergin, respectively, into the cytosol, suggesting a possible mechanism for selectively disrupting the two pathways [4].
  • Parrish attributed this term to his mentor, Dr. Phillip Syng Physick, who applied it to patients with severe lower urinary tract symptoms with no discernible etiology, with the most common etiology during the 19th century being bladder stones [5].
 

Biological context of AP1GBP1

 

Associations of AP1GBP1 with chemical compounds

  • GGAs possess four conserved functional domains, each of which interacts with cargo proteins including mannose 6-phosphate receptors, the small GTPase ARF, clathrin, or accessory proteins including Rabaptin-5 and gamma-synergin [7].
  • In this historical article, the author describes Frick's education under his two great mentors, Philip Syng Physick and George Joseph Beer, and reviews Frick's book: A Treatise on the Diseases of the Eye; Including the Doctrines and Practice of the Most Eminent Modern Surgeons, and Particularly Those of Professor Beer [8].
 

Physical interactions of AP1GBP1

 

Other interactions of AP1GBP1

  • 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 [9].

References

  1. 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]
  2. Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain. Nogi, T., Shiba, Y., Kawasaki, M., Shiba, T., Matsugaki, N., Igarashi, N., Suzuki, M., Kato, R., Takatsu, H., Nakayama, K., Wakatsuki, S. Nat. Struct. Biol. (2002) [Pubmed]
  3. The aftiphilin/p200/gamma-synergin complex. Hirst, J., Borner, G.H., Harbour, M., Robinson, M.S. Mol. Biol. Cell (2005) [Pubmed]
  4. Binding partners for the COOH-terminal appendage domains of the GGAs and gamma-adaptin. Lui, W.W., Collins, B.M., Hirst, J., Motley, A., Millar, C., Schu, P., Owen, D.J., Robinson, M.S. Mol. Biol. Cell (2003) [Pubmed]
  5. The historical origins of interstitial cystitis. Parsons, J.K., Parsons, C.L. J. Urol. (2004) [Pubmed]
  6. Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin. Kent, H.M., McMahon, H.T., Evans, P.R., Benmerah, A., Owen, D.J. Structure (Camb.) (2002) [Pubmed]
  7. The structure and function of GGAs, the traffic controllers at the TGN sorting crossroads. Nakayama, K., Wakatsuki, S. Cell Struct. Funct. (2003) [Pubmed]
  8. Frick's Treatise on the Diseases of the Eye. Albert, D.M. Survey of ophthalmology. (1987) [Pubmed]
  9. 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]
 
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