Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-6-10
pubmed:abstractText
Recent work identified ABCA1 as the major regulator of plasma HDL-cholesterol responsible for the removal of excess choline-phospholipids and cholesterol from peripheral cells and tissues. ABCA1 function may depend on the association with heteromeric proteins and to identify these candidates a human liver yeast two-hybrid library was screened with the carboxyterminal 144 amino acids of ABCA1. Beta2-syntrophin was found to interact with ABCA1 and the C-terminal five amino acids of ABCA1 proned to represent a perfect tail for binding to syntrophin PDZ domains. Immunoprecipitation further confirmed the association of ABCA1 and beta2-syntrophin and in addition utrophin, known to couple beta2-syntrophin and its PDZ ligands to the F-actin cytoskeleton, was identified as a constituent of this complex. ABCA1 in the plasmamembrane of human macrophages was found to be partially associated with Lubrol rafts and effluxed choline-phospholipids involve these microdomains. Beta2-syntrophin does not colocalize in these rafts indicating that beta2-syntrophin may participate in the retaining of ABCA1 in cytoplasmic vesicles and for the targeting of ABCA1 to plasmamembrane microdomains when ABCA1 is released from beta2-syntrophin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2002 Elsevier Science (USA).
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
293
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
759-65
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12054535-ATP-Binding Cassette Transporters, pubmed-meshheading:12054535-Adult, pubmed-meshheading:12054535-Amino Acid Sequence, pubmed-meshheading:12054535-Cell Membrane, pubmed-meshheading:12054535-Cells, Cultured, pubmed-meshheading:12054535-Cytoplasmic Vesicles, pubmed-meshheading:12054535-Cytoskeletal Proteins, pubmed-meshheading:12054535-Dystrophin-Associated Proteins, pubmed-meshheading:12054535-Fibroblasts, pubmed-meshheading:12054535-Humans, pubmed-meshheading:12054535-Macromolecular Substances, pubmed-meshheading:12054535-Membrane Proteins, pubmed-meshheading:12054535-Middle Aged, pubmed-meshheading:12054535-Molecular Sequence Data, pubmed-meshheading:12054535-Precipitin Tests, pubmed-meshheading:12054535-Protein Structure, Tertiary, pubmed-meshheading:12054535-Sequence Homology, Amino Acid, pubmed-meshheading:12054535-Two-Hybrid System Techniques, pubmed-meshheading:12054535-Utrophin
pubmed:year
2002
pubmed:articleTitle
The carboxyterminus of the ATP-binding cassette transporter A1 interacts with a beta2-syntrophin/utrophin complex.
pubmed:affiliation
Institute of Clinical Chemistry and Laboratory Medicine, University of Regensburg, Franz-Josef-Strauss-Allee 11, D-93053 Regensburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't