Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
52
pubmed:dateCreated
1996-2-8
pubmed:abstractText
The assembly of cytosolic clathrin into the cytoplasmic face of coated pits and coated vesicles appears to be driven by the clathrin-associated protein (AP) complexes. We have previously shown that one of the large chains of the AP complexes, the beta chain, is sufficient to drive coat assembly in vitro. This chain consists of two domains, the amino-terminal trunk and the carboxyl-terminal ear, linked by a "hinge." We report here that presence of the hinge in recombinant beta trunk or in recombinant beta ear fragments is essential for driving in vitro assembly of clathrin into coats. We have also used a binding assay to map the clathrin-binding site by nested deletion of hinge sequences to a 50-residue region in the center of the hinge. This sequence is conserved in all known beta sequences from multicellular organisms. The interaction of a single beta hinge with a clathrin triskelion is weak, and we propose that recruitment of cytosolic clathrin to a forming coated pit involves simultaneous contacts between the legs of single clathrin trimers and the beta hinges of two or three membrane-bound AP complexes. Uncoating is likely to require interruption of these contacts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31083-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
A clathrin-binding site in the hinge of the beta 2 chain of mammalian AP-2 complexes.
pubmed:affiliation
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't