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Titolo:
Molecular cloning and characterization of Pals, proteins associated with mLin-7
Autore:
Kamberov, E; Makarova, O; Roh, M; Liu, A; Karnak, D; Straight, S; Margolis, B;
Indirizzi:
Univ Michigan, Med Ctr, 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, Med Ctr, Dept Internal Med, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 nternal Med, Ann Arbor, MI 48109 USA Univ Michigan, Med Ctr, 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 BIOLOGICAL CHEMISTRY
fascicolo: 15, volume: 275, anno: 2000,
pagine: 11425 - 11431
SICI:
0021-9258(20000414)275:15<11425:MCACOP>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYNAPTIC VESICLE EXOCYTOSIS; ELEGANS VULVAR INDUCTION; BASOLATERAL MEMBRANE; SIGNALING COMPLEX; EPITHELIAL-CELLS; DOMAINS; GENE; LOCALIZATION; ENCODES; HOMOLOG;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Margolis, B Univ Michigan, Med Ctr, Howard Hughes Med Inst, Rm 4570,MSRB 2,1150 W Med Ctr Dr, Ann Arbor, MI 48109 USA Univ Michigan Rm 4570,MSRB 2,1150 W Med Ctr Dr Ann Arbor MI USA 48109
Citazione:
E. Kamberov et al., "Molecular cloning and characterization of Pals, proteins associated with mLin-7", J BIOL CHEM, 275(15), 2000, pp. 11425-11431

Abstract

In Caenorhabditis elegans, three PDZ domain proteins, Lin-2, Lin-7, and Lin-10, are necessary for the proper targeting of the Let-23 growth factor receptor to the basolateral surface of epithelial cells. It has been demonstrated that homologues of Lin-2, Lin-7, and Lin-10 form a heterotrimeric complex in mammalian brain. Using Far Western overlay assay, we have identifiedadditional proteins that can bind to the amino terminus of mLin-7 and cloned the genes encoding these proteins using bacterial expression cloning. Wecall these proteins Pals, for proteins associated with Lin-7. These proteins, which include mammalian Lin-2, contain a conserved mLin-7 binding domain in addition to guanylate kinase, PDZ (postsynaptic density 95/discs large/zona occludens-1), and Src homology 3 domains. Using site-directed mutagenesis, we have identified the conserved residues among these proteins crucial for mLin-7 binding. Two of these proteins, Pals1 and Pals2, are newly described. Pals1 consists of 675 amino acids and maps to mouse chromosome 12. Pals2 was found to exist in two splice forms of 539 and 553 amino acids andmaps to mouse chromosome 6. Like mLin-2, Pals1 and Pals2 localize to the lateral membrane in Madin-Darby canine kidney cells. Pals proteins representa new subfamily of membrane-associated guanylate kinases that allow for multiple targeting complexes containing mLin-7.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 15:00:11