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Titolo:
The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes
Autore:
Patrie, KM; Drescher, AJ; Goyal, M; Wiggins, RC; Margolis, B;
Indirizzi:
Univ Michigan, Howard Hughes Med Inst, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 es Med Inst, Ann Arbor, MI 48109 USA Univ Michigan, Dept Internal Med, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 nternal Med, Ann Arbor, MI 48109 USA Univ Michigan, Dept Biol Chem, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 t Biol Chem, Ann Arbor, MI 48109 USA
Titolo Testata:
JOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY
fascicolo: 4, volume: 12, anno: 2001,
pagine: 667 - 677
SICI:
1046-6673(200104)12:4<667:TMGKPM>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR-ASSOCIATED PROTEIN; AMYLOID PRECURSOR PROTEIN; PDZ DOMAIN; HEYMANN NEPHRITIS; EPITHELIAL-CELLS; GENE FAMILY; INTERACTS; LOCALIZATION; CLONING; GP330;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Margolis, B Univ Michigan, Howard Hughes Med Inst, 4570 MSRB 2,Box 0650,1150 W Med CtrDr, Ann Arbor, MI 48109 USA Univ Michigan 4570 MSRB 2,Box 0650,1150 W Med Ctr Dr Ann Arbor MI USA 48109
Citazione:
K.M. Patrie et al., "The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes", J AM S NEPH, 12(4), 2001, pp. 667-677

Abstract

The transmembrane endocytic receptor glycoprotein 330/megalin thereafter referred to as megalin) is localized to the apical membrane domain of epithelial cells, where it is involved in the uptake of proteins from extracellular sources. The cytoplasmic domain of megalin contains amino acid motifs that have the potential to bind to other proteins, which may influence its localization or function. The yeast two-hybrid system was used to search for proteins that bind to the cytoplasmic tail of megalin, and a protein fragment from a mouse embryonic cDNA library that contained a single PDZ domain was identified. This protein, which was named glycoprotein 330-associated protein (GASP), appears to be a truncated mouse counterpart of the human and rat proteins atrophin-1-interacting protein-1 and synaptic scaffolding molecule, respectively. The interaction of GASP with megalin is mediated by thePDZ domain of GASP binding to the DSDV motif found at the carboxyl-terminus of megalin. A mutant version of megalin that lacks the terminal valine isunable to bind to GASP, illustrating the PDZ domain-dependent interaction between these two proteins. A close homolog of GASP, i.e., membrane-associated guanylate kinase with inverted orientation-1 (MAGI-1), is more ubiquitous in its tissue distribution (including kidney) and is also able to specifically bind to megalin via its fifth PDZ domain. Immunofluorescence studiesof adult kidney revealed that MAGI-1 is expressed in the glomerulus of thekidney, in a manner that parallels the expression of the podocyte-specificprotein glomerular epithelial protein 1. Western analysis of endogenous MAGI-1 from glomerular preparations suggests that it is associated with the cytoskeleton and seems to be expressed in a different form, compared with cell line-derived endogenous MAGI-1. The association of megalin with MAGI-1 may allow the assembly of a multiprotein complex, in which megalin may servea nonendocytic function in glomerular podocytes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 21:46:20