Linked Life Data

11093251

Source:http://linkedlifedata.com/resource/pubmed/id/11093251

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-12-18
pubmed:abstractText
When enteropathogenic Escherichia coli (EPEC) attach and infect host cells, they induce a cytoskeletal rearrangement and the formation of cytoplasmic columns of actin filaments called pedestals. The attached EPEC and pedestals move over the surface of the host cell in an actin-dependent reaction [Sanger et al., 1996: Cell Motil Cytoskeleton 34:279-287]. The discovery that EPEC inserts the protein, translocated intimin receptor (Tir), into the membrane of host cells, where it binds the EPEC outer membrane protein, intimin [Kenny et al., 1997: Cell 91:511-520], suggests Tir serves two functions: tethering the bacteria to the host cell and providing a direct connection to the host's cytoskeleton. The sequence of Tir predicts a protein of 56.8 kD with three domains separated by two predicted trans-membrane spanning regions. A GST-fusion protein of the N-terminal 233 amino acids of Tir (Tir1) binds to alpha-actinin, talin, and vinculin from cell extracts. GST-Tir1 also coprecipitates purified forms of alpha-actinin, talin, and vinculin while GST alone does not bind these three focal adhesion proteins. Biotinylated probes of these three proteins also bound Tir1 cleaved from GST. Similar associations of alpha-actinin, talin, and vinculin were also detected with the C-terminus of Tir, i.e., Tir3, the last 217 amino acids. Antibody staining of EPEC-infected cultured cells reveals the presence of focal adhesion proteins beneath the attached bacteria. Our experiments support a model in which the cytoplasmic domains of Tir recruit a number of focal adhesion proteins that can bind actin filaments to form pedestals. Since pedestals also contain villin, tropomyosin and myosin II [Sanger et al., 1996: Cell Motil. Cytoskeleton 34:279-287], the pedestals appear to be a novel structure sharing properties of both focal adhesions and microvilli.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0886-1544
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
307-18
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11093251-Actinin, pubmed-meshheading:11093251-Amino Acid Sequence, pubmed-meshheading:11093251-Biotinylation, pubmed-meshheading:11093251-Cytoplasm, pubmed-meshheading:11093251-Escherichia coli, pubmed-meshheading:11093251-Escherichia coli Proteins, pubmed-meshheading:11093251-Focal Adhesions, pubmed-meshheading:11093251-Glutathione Transferase, pubmed-meshheading:11093251-Microscopy, Confocal, pubmed-meshheading:11093251-Microscopy, Fluorescence, pubmed-meshheading:11093251-Models, Biological, pubmed-meshheading:11093251-Molecular Sequence Data, pubmed-meshheading:11093251-Precipitin Tests, pubmed-meshheading:11093251-Protein Binding, pubmed-meshheading:11093251-Protein Structure, Tertiary, pubmed-meshheading:11093251-Receptors, Cell Surface, pubmed-meshheading:11093251-Recombinant Fusion Proteins, pubmed-meshheading:11093251-Sequence Homology, Amino Acid, pubmed-meshheading:11093251-Talin, pubmed-meshheading:11093251-Vinculin
pubmed:year
2000
pubmed:articleTitle
Interaction of the enteropathogenic Escherichia coli protein, translocated intimin receptor (Tir), with focal adhesion proteins.
pubmed:affiliation
Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia 19104-6058, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't