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AP180 is a protein that plays an important role in clathrin-mediated endocytosis of synaptic vesicles. It is capable of simultaneously binding both membrane lipids (via an ANTH domain) and clathrin and is therefore thought to recruit clathrin to the membrane of newly invaginating vesicles. In Drosophila (fruit flies), deletion of the AP180 homologue, leads to enlarged but much fewer vesicles and an overall decrease in transmitter release. In Drosophila it was also shown that AP180 is also required for either recycling vesicle proteins and/or maintaining the distribution of both vesicle and synaptic proteins in the nerve terminal. A ubiquitous form of the protein in mammals, CALM, (Clathrin-assembly lymphoid myeloid leukaemia protein) is named after its association with myeloid and lymphoid leukemias where some translocations map to this gene. The C-terminus of AP180 is a powerful and specific inhibitor of clathrin-mediated endocytosis.
Additional recommended knowledge
More information is found on endocytosis.org.
Ford, M.G.J., Pearse, B., Higgins, M., Vallis, Y., Owen, D., Gibson, A., Hopkins, C.R., Evans, P.R. and McMahon, H.T. (2001) Simultaneous binding of PI (4,5)P2 and clathrin by AP180 causes nucleation of clathrin lattices on membranes. Science 291, 1051-1055. pubmed
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Ap180". A list of authors is available in Wikipedia.|