Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-10-11
pubmed:abstractText
Uncoating of clathrin-coated vesicles in neuronal cells requires hsc70 in concert with the cofactor auxilin which contains a J-domain as well as a domain with homology to dual specific phosphatases and tensin, known as PTEN. The question of whether an analogous factor operates in other cell types has until now remained unanswered. Here we show that it is the recently discovered and widely expressed cyclin G-associated protein kinase which fulfils the function of neuronal auxilin in hsc70-mediated clathrin coat dissociation. GAK possesses a J-domain, which stimulates the hsc70 ATPase, it competes with auxilin for clathrin binding and at sufficiently high concentrations acts as a clathrin assembly protein. Moreover, GAK binds to the gamma- and alpha-appendage domains of the adaptor proteins AP-1 and AP-2 in vitro and phosphorylates their medium chains. Cells that transiently overexpress GAK are impaired in respect of receptor-mediated endocytosis. In transfected cells clathrin is dislodged from coated pits/vesicles and co-localizes with GFP-GAK in the form of large aggregates. The cellular distribution of membrane-associated adaptors was unaffected by overexpression of GAK. Our results point to a hsc70/auxilin-based uncoating system as a ubiquitous feature of eukaryotic cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CCNG1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ccng1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Clathrin, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin G, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin G1, http://linkedlifedata.com/resource/pubmed/chemical/Cyclins, http://linkedlifedata.com/resource/pubmed/chemical/GAK protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Gak protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/HSC70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSPA8 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Hspa8 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0171-9335
pubmed:author
pubmed:issnType
Print
pubmed:volume
79
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
336-42
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10887964-Animals, pubmed-meshheading:10887964-Carrier Proteins, pubmed-meshheading:10887964-Cell Fractionation, pubmed-meshheading:10887964-Clathrin, pubmed-meshheading:10887964-Clathrin-Coated Vesicles, pubmed-meshheading:10887964-Cyclin G, pubmed-meshheading:10887964-Cyclin G1, pubmed-meshheading:10887964-Cyclins, pubmed-meshheading:10887964-Endocytosis, pubmed-meshheading:10887964-Genes, Reporter, pubmed-meshheading:10887964-HSC70 Heat-Shock Proteins, pubmed-meshheading:10887964-HSP70 Heat-Shock Proteins, pubmed-meshheading:10887964-HeLa Cells, pubmed-meshheading:10887964-Humans, pubmed-meshheading:10887964-Immunohistochemistry, pubmed-meshheading:10887964-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:10887964-Molecular Chaperones, pubmed-meshheading:10887964-Phosphorylation, pubmed-meshheading:10887964-Protein Binding, pubmed-meshheading:10887964-Protein Structure, Tertiary, pubmed-meshheading:10887964-Protein-Serine-Threonine Kinases, pubmed-meshheading:10887964-Radioligand Assay, pubmed-meshheading:10887964-Rats, pubmed-meshheading:10887964-Recombinant Fusion Proteins, pubmed-meshheading:10887964-Transfection
pubmed:year
2000
pubmed:articleTitle
Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation.
pubmed:affiliation
Department of Cell Biology, Centre of Anatomy, Hannover Medical School, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't