Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1998-11-18
pubmed:abstractText
Several end mutations that block the internalisation step of endocytosis in Saccharomyces cerevisiae also affect the cortical actin cytoskeleton [1]. END5 encodes a proline-rich protein (End5p or verprolin) required for a polarised cortical actin cytoskeleton and endocytosis [2,3]. End5p interacts with actin [4], but its exact function is not yet known. To help elucidate End5p function, we sought other End5p-interacting proteins and identified the LAS17/BEE1 gene (encoding the yeast homologue of the human Wiskott-Aldrich Syndrome protein, WASp) as a high-copy-number suppressor of the temperature-sensitive growth and endocytic defects of end5-1 cells (carrying a frameshift mutation affecting the last 213 residues of End5p). LAS17 is unable to suppress a full deletion of END5 (end5 delta), however, suggesting that the defective End5-1p in end5-1 mutants may be stabilised by Las17p. The amino terminus of Las17p interacts with the carboxyl terminus of End5p in the yeast two-hybrid system and similar interactions have been shown between WASp and a mammalian End5p homologue, WASp-interacting protein (WIP) [5]. As las17 delta deletion mutants are blocked in endocytosis, we conclude that Las17p and End5p interact and are essential for endocytosis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/LAS17 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/VRP1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/WASL protein, human, http://linkedlifedata.com/resource/pubmed/chemical/WIPF1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Wiskott-Aldrich Syndrome Protein, http://linkedlifedata.com/resource/pubmed/chemical/Wiskott-Aldrich Syndrome Protein...
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0960-9822
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
959-62
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:9742397-Carrier Proteins, pubmed-meshheading:9742397-Cytoskeletal Proteins, pubmed-meshheading:9742397-Endocytosis, pubmed-meshheading:9742397-Frameshift Mutation, pubmed-meshheading:9742397-Fungal Proteins, pubmed-meshheading:9742397-Gene Dosage, pubmed-meshheading:9742397-Genes, Fungal, pubmed-meshheading:9742397-Humans, pubmed-meshheading:9742397-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:9742397-Microfilament Proteins, pubmed-meshheading:9742397-Nerve Tissue Proteins, pubmed-meshheading:9742397-Recombinant Fusion Proteins, pubmed-meshheading:9742397-Saccharomyces cerevisiae, pubmed-meshheading:9742397-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9742397-Sequence Deletion, pubmed-meshheading:9742397-Suppression, Genetic, pubmed-meshheading:9742397-Temperature, pubmed-meshheading:9742397-Wiskott-Aldrich Syndrome, pubmed-meshheading:9742397-Wiskott-Aldrich Syndrome Protein, pubmed-meshheading:9742397-Wiskott-Aldrich Syndrome Protein, Neuronal
pubmed:year
1998
pubmed:articleTitle
The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast.
pubmed:affiliation
Institute of Molecular Agrobiology, National University of Singapore, Republic of Singapore.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't