|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
10
|
|
pubmed:dateCreated |
2003-9-5
|
|
pubmed:abstractText |
An expression screen of a rat cDNA library for sequences encoding Golgi-localized integral membrane proteins identified a protein with an apparent novel topology, i.e. with both an N-terminal transmembrane domain and a C-terminal glycosyl-phosphatidylinositol (GPI) anchor. Our data are consistent with this. Thus, the protein would have a topology that, in mammalian cells, is shared only by a minor, but pathologically important, topological isoform of the prion protein (PrP). The human orthologue of this protein has been described previously (BST-2 or HM1.24 antigen) as a cell surface molecule that appears to be involved in early pre-B-cell development and which is present at elevated levels at the surface of myeloma cells. We show that rat BST-2/HM1.24 has both a cell surface and an intracellular (juxtanuclear) location and is efficiently internalized from the cell surface. We also show that the cell surface pool of BST-2/HM1.24 is predominantly present in the apical plasma membrane of polarized cells. The fact that rat BST-2/HM1.24 apparently possesses a GPI anchor led us to speculate that it might exist in cholesterol-rich lipid microdomains (lipid rafts) at the plasma membrane. Data from several experiments are consistent with this localization. We present a model in which BST-2/HM1.24 serves to link adjacent lipid rafts within the plasma membrane.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
1398-9219
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
4
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
694-709
|
|
pubmed:dateRevised |
2010-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:12956872-Amino Acid Sequence,
pubmed-meshheading:12956872-Animals,
pubmed-meshheading:12956872-Antibodies, Monoclonal,
pubmed-meshheading:12956872-Antigens, Surface,
pubmed-meshheading:12956872-COS Cells,
pubmed-meshheading:12956872-Cell Line,
pubmed-meshheading:12956872-Cercopithecus aethiops,
pubmed-meshheading:12956872-Conserved Sequence,
pubmed-meshheading:12956872-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:12956872-GPI-Linked Proteins,
pubmed-meshheading:12956872-Male,
pubmed-meshheading:12956872-Membrane Glycoproteins,
pubmed-meshheading:12956872-Membrane Microdomains,
pubmed-meshheading:12956872-Membrane Proteins,
pubmed-meshheading:12956872-Microscopy, Confocal,
pubmed-meshheading:12956872-Microscopy, Fluorescence,
pubmed-meshheading:12956872-Models, Biological,
pubmed-meshheading:12956872-Molecular Sequence Data,
pubmed-meshheading:12956872-Protein Structure, Tertiary,
pubmed-meshheading:12956872-Rats,
pubmed-meshheading:12956872-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12956872-Sequence Homology, Amino Acid,
pubmed-meshheading:12956872-Tissue Distribution
|
|
pubmed:year |
2003
|
|
pubmed:articleTitle |
Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology.
|
|
pubmed:affiliation |
Department of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
