In:
Science, American Association for the Advancement of Science (AAAS), Vol. 291, No. 5506 ( 2001-02-09), p. 1051-1055
Abstract:
Adaptor protein 180 (AP180) and its homolog, clathrin assembly lymphoid myeloid leukemia protein (CALM), are closely related proteins that play important roles in clathrin-mediated endocytosis. Here, we present the structure of the NH 2 -terminal domain of CALM bound to phosphatidylinositol-4,5- bisphosphate [PtdIns(4,5)P 2 ] via a lysine-rich motif. This motif is found in other proteins predicted to have domains of similar structure (for example, Huntingtin interacting protein 1). The structure is in part similar to the epsin NH 2 -terminal (ENTH) domain, but epsin lacks the PtdIns(4,5)P 2 -binding site. Because AP180 could bind to PtdIns(4,5)P 2 and clathrin simultaneously, it may serve to tether clathrin to the membrane. This was shown by using purified components and a budding assay on preformed lipid monolayers. In the presence of AP180, clathrin lattices formed on the monolayer. When AP2 was also present, coated pits were formed.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.291.5506.1051
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
2001
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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