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Gene Review

SNAP91  -  synaptosomal-associated protein, 91kDa

Homo sapiens

Synonyms: 91 kDa synaptosomal-associated protein, AP180, CALM, Clathrin coat assembly protein AP180, Clathrin coat-associated protein AP180, ...
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Psychiatry related information on SNAP91


High impact information on SNAP91

  • Structurally, this domain, combined with the preceding VHS domain, resembles CALM, an AP180 homolog involved in endocytosis [2].
  • We have also defined the binding sites for Eps15 on squid AP180 [3].
  • We demonstrate that AP180 and auxilin compete for binding to the alpha-ear domain of AP-2 [4].
  • Like AP180, auxilin also directly interacts with the ear domain of beta-adaptin [4].
  • Epsin and AP180/CALM are endocytotic accessory proteins that have been implicated in the formation of clathrin-coated pits [5].

Biological context of SNAP91

  • AP-3 (AP180) in rat sympathetic neurons maintained in culture was analyzed by pulse-chase labeling with [35S]methionine to look for post-translational modifications [6].
  • Expression of auxilin or AP180 inhibits endocytosis by mislocalizing clathrin: evidence for formation of nascent pits containing AP1 or AP2 but not clathrin [7].
  • The amino acid sequence of peptide derived from the purified protein is now identified as AP180, a clathrin assembly protein that has been implicated in clathrin-mediated synaptic vesicle recycling in synapses [8].

Anatomical context of SNAP91

  • AP180 is efficient in facilitating the formation of clathrin-coated vesicles and regulating their size, but its exact location in synapse is not clear [9].
  • Clathrin assembly protein AP180 plays a regulatory role in clathrin-mediated synaptic vesicle recycling in synapses [1].
  • Previously, using immunoblot analysis, we observed a significant reduction of AP180 protein in Alzheimer's disease neocortex [1].
  • Overall, AP180 was revealed as immunoreactive punctate granules located in the neuropil, and around neuronal cell bodies and their processes, consistent with the typical expression of synaptic proteins [1].
  • In addition, AP180 immunoreactivity in the molecular layer of the dentate gyrus showed several changes in Alzheimer's disease [1].

Associations of SNAP91 with chemical compounds

  • Furthermore, ultrastructural analysis of primate retina showed that AP180 immunoreactivity was preferentially and highly enriched at ribbon synapses, where glutamate is released tonically at high levels and rapid vesicle turnover is essential [10].

Regulatory relationships of SNAP91


Other interactions of SNAP91

  • These results can be explained by the binding of amphiphysin to the NH(2)-terminal domain of clathrin and by a competition with the binding of this domain to the beta-subunit of AP-2 and AP180 [12].
  • In this study, we compared the expression of AP180 with synaptophysin in the aged human brain using confocal immunofluorescence microscopy [9].
  • The clathrin assembly lymphoid myeloid leukemia (CALM) gene encodes a putative homologue of the clathrin assembly synaptic protein AP180 [13].
  • However, expression of auxilin with its J-domain mutated so that it no longer interacted with Hsc70 also inhibited endocytosis as did expression of the clathrin-assembly protein, AP180, or its clathrin-binding domain [7].
  • In this report, we demonstrate the stable association of PLCgamma1 with AP180 in a clathrin-coated vesicle complex, which not only binds to the carboxyl-terminal SH2 domain of PLCgamma1, but also inhibits its enzymatic activity in a dose-dependent manner [8].

Analytical, diagnostic and therapeutic context of SNAP91


  1. Changes in synaptic expression of clathrin assembly protein AP180 in Alzheimer's disease analysed by immunohistochemistry. Yao, P.J., Morsch, R., Callahan, L.M., Coleman, P.D. Neuroscience (1999) [Pubmed]
  2. Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport. Shiba, T., Kawasaki, M., Takatsu, H., Nogi, T., Matsugaki, N., Igarashi, N., Suzuki, M., Kato, R., Nakayama, K., Wakatsuki, S. Nat. Struct. Biol. (2003) [Pubmed]
  3. Eps15 homology domain-NPF motif interactions regulate clathrin coat assembly during synaptic vesicle recycling. Morgan, J.R., Prasad, K., Jin, S., Augustine, G.J., Lafer, E.M. J. Biol. Chem. (2003) [Pubmed]
  4. Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin. Scheele, U., Alves, J., Frank, R., Duwel, M., Kalthoff, C., Ungewickell, E. J. Biol. Chem. (2003) [Pubmed]
  5. Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. Stahelin, R.V., Long, F., Peter, B.J., Murray, D., De Camilli, P., McMahon, H.T., Cho, W. J. Biol. Chem. (2003) [Pubmed]
  6. Clathrin assembly protein AP-3 is phosphorylated and glycosylated on the 50-kDa structural domain. Murphy, J.E., Hanover, J.A., Froehlich, M., DuBois, G., Keen, J.H. J. Biol. Chem. (1994) [Pubmed]
  7. Expression of auxilin or AP180 inhibits endocytosis by mislocalizing clathrin: evidence for formation of nascent pits containing AP1 or AP2 but not clathrin. Zhao, X., Greener, T., Al-Hasani, H., Cushman, S.W., Eisenberg, E., Greene, L.E. J. Cell. Sci. (2001) [Pubmed]
  8. AP180 binds to the C-terminal SH2 domain of phospholipase C-gamma1 and inhibits its enzymatic activity. Han, S.J., Lee, J.H., Hong, S.H., Park, S.D., Kim, C.G., Song, M.D., Park, T.K., Kim, C.G. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  9. Immunohistochemical characterization of clathrin assembly protein AP180 and synaptophysin in human brain. Yao, P.J., O'Herron, T.M., Coleman, P.D. Neurobiol. Aging (2003) [Pubmed]
  10. High-resolution localization of clathrin assembly protein AP180 in the presynaptic terminals of mammalian neurons. Yao, P.J., Coleman, P.D., Calkins, D.J. J. Comp. Neurol. (2002) [Pubmed]
  11. Effect of clathrin assembly lymphoid myeloid leukemia protein depletion on clathrin coat formation. Meyerholz, A., Hinrichsen, L., Groos, S., Esk, P.C., Brandes, G., Ungewickell, E.J. Traffic (2005) [Pubmed]
  12. Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites. Slepnev, V.I., Ochoa, G.C., Butler, M.H., De Camilli, P. J. Biol. Chem. (2000) [Pubmed]
  13. Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic. Tebar, F., Bohlander, S.K., Sorkin, A. Mol. Biol. Cell (1999) [Pubmed]
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