Abstract：
:Clathrin-mediated endocytosis plays a major role in retrieving synaptic vesicles from the plasma membrane following exocytosis. This endocytic process requires AP180 (or a homolog), which promotes the assembly and restricts the size of clathrin-coated vesicles. The highly conserved 33 kDa amino-terminal domain of AP180 plays a critical role in binding to phosphoinositides and in regulating the clathrin assembly activity of AP180. The crystal structure of the amino-terminal domain reported herein reveals a novel fold consisting of a large double layer of sheets of ten alpha helices and a unique site for binding phosphoinositides. The finding that the clathrin-box motif is mostly buried and lies in a helix indicates a different site and mechanism for binding of the domain to clathrins than previously assumed.
journal_name
Celljournal_title
Cellauthors
Mao Y,Chen J,Maynard JA,Zhang B,Quiocho FAdoi
10.1016/s0092-8674(01)00230-6subject
Has Abstractpub_date
2001-02-09 00:00:00pages
433-40issue
3eissn
0092-8674issn
1097-4172pii
S0092-8674(01)00230-6journal_volume
104pub_type
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