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Titolo:
Defective organellar membrane protein trafficking in Ap3b1-deficient cells
Autore:
Yang, W; Li, CY; Ward, DM; Kaplan, J; Mansour, SL;
Indirizzi:
Univ Utah, Dept Human Genet, Salt Lake City, UT 84112 USA Univ Utah Salt Lake City UT USA 84112 Genet, Salt Lake City, UT 84112 USA Univ Utah, Dept Pathol, Salt Lake City, UT 84112 USA Univ Utah Salt Lake City UT USA 84112 athol, Salt Lake City, UT 84112 USA
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 22, volume: 113, anno: 2000,
pagine: 4077 - 4086
SICI:
0021-9533(200011)113:22<4077:DOMPTI>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
AP-3 ADAPTER COMPLEX; HERMANSKY-PUDLAK-SYNDROME; EMBRYONIC STEM-CELLS; ALKALINE-PHOSPHATASE; CONFERS RESISTANCE; SYNAPTIC VESICLES; EXPRESSION; MOUSE; ZINC; SUBUNIT;
Keywords:
mouse mutant; gene targeting; Hermansky-Pudlak syndrome; lamp protein; lysosome; melanosome; tyrosinase; zinc transporter;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Mansour, SL Univ Utah, Dept Human Genet, Salt Lake City, UT 84112 USA UnivUtah Salt Lake City UT USA 84112 Lake City, UT 84112 USA
Citazione:
W. Yang et al., "Defective organellar membrane protein trafficking in Ap3b1-deficient cells", J CELL SCI, 113(22), 2000, pp. 4077-4086

Abstract

AP-3 is a heterotetrameric protein complex involved in intracellular vesicle transport. Molecular analyses show that Ap3b1, which encodes the AP-3 beta 3A subunit, is altered in pearl mice. To provide genetic evidence that mutation of Ap3b1 is responsible for the pearl phenotype and to determine the null phenotype, the Ap3b1 gene was disrupted by homologous recombination,Mice homozygous for the resulting allele, Ap3b1(LN), or compound heterozygotes with pearl, displayed phenotypes similar to those of pearl mice, confirming that Ap3b1 is the causal gene for pearl. Moreover, pearl is likely tobe a hypomorph as the Ap3b1(LN) homozygotes had a lighter coat color and accumulated fewer of the mu3 and delta3 subunits of AP-3 than did pearl mice. Finally, immunofluorescence analysis of fibroblasts and melanocytes cultured from Ap3b1(LN) homozygotes revealed that the lysosomal membrane proteins Lamp I and Lamp II and the melanosomal membrane protein tyrosinase were mislocalized. In particular, the Lamp proteins were clustered on the cell surface. These findings strengthen the evidence for an alternate pathway via the plasma membrane for cargo normally transported to organelles by AP-3.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 04:56:19