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
|