- 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 NH2-terminal domain of CALM bound to phosphatidylinositol-4,5- bisphosphate [PtdIns(4,5)P2] 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 ...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1126/science.291.5506.1051
-
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- Journal:
- Science (New York, N.Y.)
- Volume:
- 291
- Issue:
- 5506
- Pages:
- 1051-1055
- Publication date:
- 2001-02-05
- DOI:
- EISSN:
-
1095-9203
- ISSN:
-
0036-8075
- URN:
-
uuid:3d1ffdab-bf4a-4a18-9409-8b191e4d83d9
- Source identifiers:
-
196865
- Local pid:
- pubs:196865
- Language:
- English
- Keywords:
- Copyright date:
- 2001
Journal article
Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes.
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