Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2002-8-14
pubmed:databankReference
pubmed:abstractText
The AP1 complex is one of a family of heterotetrameric clathrin-adaptor complexes involved in vesicular trafficking between the Golgi and endosomes. The complex has two large subunits, gamma and beta1, which can be divided into trunk, hinge, and appendage domains. The 1.8 A resolution structure of the gamma appendage is presented. The binding site for the known gamma appendage ligand gamma-synergin is mapped through creation of point mutations designed on the basis of the structure. We also show that Eps15, a protein believed to be involved in vesicle formation at the plasma membrane, is also a ligand of gamma appendage and binds to the same site as gamma-synergin. This observation explains the demonstrated brefeldinA (BFA)-sensitive colocalization of Eps15 and AP1 at the Golgi complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex 1, http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex gamma..., http://linkedlifedata.com/resource/pubmed/chemical/Brefeldin A, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/EPS15 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Eps15 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Synthesis Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SYNRG protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Syng protein, rat
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1139-48
pubmed:dateRevised
2011-7-20
pubmed:meshHeading
pubmed-meshheading:12176391-Adaptor Protein Complex 1, pubmed-meshheading:12176391-Adaptor Protein Complex gamma Subunits, pubmed-meshheading:12176391-Amino Acid Sequence, pubmed-meshheading:12176391-Animals, pubmed-meshheading:12176391-Binding Sites, pubmed-meshheading:12176391-Brefeldin A, pubmed-meshheading:12176391-Calcium-Binding Proteins, pubmed-meshheading:12176391-Carrier Proteins, pubmed-meshheading:12176391-Crystallography, X-Ray, pubmed-meshheading:12176391-Golgi Apparatus, pubmed-meshheading:12176391-HeLa Cells, pubmed-meshheading:12176391-Humans, pubmed-meshheading:12176391-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:12176391-Ligands, pubmed-meshheading:12176391-Mice, pubmed-meshheading:12176391-Models, Molecular, pubmed-meshheading:12176391-Molecular Sequence Data, pubmed-meshheading:12176391-Molecular Structure, pubmed-meshheading:12176391-Phosphoproteins, pubmed-meshheading:12176391-Point Mutation, pubmed-meshheading:12176391-Protein Conformation, pubmed-meshheading:12176391-Protein Folding, pubmed-meshheading:12176391-Protein Synthesis Inhibitors, pubmed-meshheading:12176391-Rats, pubmed-meshheading:12176391-Recombinant Fusion Proteins, pubmed-meshheading:12176391-Sequence Alignment
pubmed:year
2002
pubmed:articleTitle
Gamma-adaptin appendage domain: structure and binding site for Eps15 and gamma-synergin.
pubmed:affiliation
MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't