Linked Life Data

15158445

Source:http://linkedlifedata.com/resource/pubmed/id/15158445

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-5-25
pubmed:abstractText
D-Lactate dehydrogenase protein 2 [Yeast 15 (1999) 1377; Biochem. Biophys. Res. Commun. 295 (2002) 910] was initially identified as the actin interacting protein 2 (Aip2p) using a two-hybrid screen to search for proteins that interact with actin [Nat. Struct. Biol. 2 (1995) 28], but no other evidence indicating an interaction between Aip2p and actin cytoskeleton has been reported so far. During our search for the protein conformation modifying activity, we serendipitously identified Aip2p isolated from Saccharomyces cerevisiae as exhibiting an interaction with F-actin both in vitro and in vivo. Incubation with Aip2p facilitated the formation of the circular form of F-actin in vitro, which exhibited an aberrant trypsin susceptibility. Overexpression of Aip2p induced multi-buds in yeast cells, whereas reduced expression interfered with the formation of the cleavage furrow for the cell division, which was rescued by the introduction of wild-type Aip2p. While Aip2p-treated F-actin in the circular form was negligibly stained by rhodamine-labeled phalloidin (rhodamine-phalloidin) in vitro, rhodamine-phalloidin staining profiles in actin interacting protein 2 gene (AIP2)-modified cells suggested a correlation between the conformation of F-actin and the expression of Aip2p in vivo. AIP2-deleted cells became sensitive to osmotic conditions, a hallmark of actin dysfunction. Finally, immunoprecipitation of yeast cells using anti-Aip2p antibody demonstrated that Aip2p associates with actin. These properties suggest that Aip2p may interact with F-actin in vivo and play an important role in the yeast cell morphology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
319
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
78-82
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15158445-Actins, pubmed-meshheading:15158445-Cell Division, pubmed-meshheading:15158445-Cytoskeleton, pubmed-meshheading:15158445-Histidine, pubmed-meshheading:15158445-L-Lactate Dehydrogenase, pubmed-meshheading:15158445-L-Lactate Dehydrogenase (Cytochrome), pubmed-meshheading:15158445-Lactate Dehydrogenases, pubmed-meshheading:15158445-Microscopy, Fluorescence, pubmed-meshheading:15158445-Osmosis, pubmed-meshheading:15158445-Phalloidine, pubmed-meshheading:15158445-Precipitin Tests, pubmed-meshheading:15158445-Protein Binding, pubmed-meshheading:15158445-Protein Conformation, pubmed-meshheading:15158445-Rhodamines, pubmed-meshheading:15158445-Saccharomyces cerevisiae, pubmed-meshheading:15158445-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15158445-Trypsin, pubmed-meshheading:15158445-Two-Hybrid System Techniques
pubmed:year
2004
pubmed:articleTitle
Interaction of D-lactate dehydrogenase protein 2 (Dld2p) with F-actin: implication for an alternative function of Dld2p.
pubmed:affiliation
Department of Cortical Function Disorders, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't