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Titolo:
AP-3 mediates tyrosinase but not TRP-1 trafficking in human melanocytes
Autore:
Huizing, M; Sarangarajan, R; Strovel, E; Zhao, Y; Gahl, WA; Boissy, RE;
Indirizzi:
Univ Cincinnati, Dept Dermatol, Cincinnati, OH 45267 USA Univ Cincinnati Cincinnati OH USA 45267 ermatol, Cincinnati, OH 45267 USA NICHHD, Sect Human Biochem Genet, Heritable Disorders Branch, NIH, Bethesda, MD 20892 USA NICHHD Bethesda MD USA 20892 isorders Branch, NIH, Bethesda, MD 20892 USA
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 7, volume: 12, anno: 2001,
pagine: 2075 - 2085
SICI:
1059-1524(200107)12:7<2075:AMTBNT>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
HERMANSKY-PUDLAK-SYNDROME; PIGMENT GRANULE BIOGENESIS; PROTEIN COMPLEX; ADAPTER COMPLEX; CYTOPLASMIC TAIL; LATE ENDOSOMES; OCULOCUTANEOUS ALBINISM; LOCUS HETEROGENEITY; VESICLE FORMATION; SORTING SIGNALS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Boissy, RE Univ Cincinnati, Dept Dermatol, Cincinnati, OH 45267 USA Univ Cincinnati Cincinnati OH USA 45267 ncinnati, OH 45267 USA
Citazione:
M. Huizing et al., "AP-3 mediates tyrosinase but not TRP-1 trafficking in human melanocytes", MOL BIOL CE, 12(7), 2001, pp. 2075-2085

Abstract

Patients with Hermansky-Pudlak syndrome type 2 (HPS-2) have mutations in the beta 3A subunit of adaptor complex-3 (AP-3) and functional deficiency ofthis complex. AP-3 serves as a coat protein in the formation of new vesicles, including, apparently, the platelet's dense body and the melanocyte's melanosome. We used HPS-2 melanocytes in culture to determine the role of AP-3 in the trafficking of the melanogenic proteins tyrosinase and tyrosinase-related protein-1 (TRP-1). TRP-1 displayed a typical melanosomal pattern in both normal and HPS-2 melanocytes. In contrast, tyrosinase exhibited a melanosomal (i.e., perinuclear and dendritic) pattern in normal cells but only a perinuclear pattern in the HPS-2 melanocytes. In addition, tyrosinase exhibited a normal pattern of expression in HPS-2 melanocytes transfected with a cDNA encoding the beta 3A subunit of the AP-3 complex. This suggests arole for AP-3 in the normal trafficking of tyrosinase to premelanosomes, consistent with the presence of a dileucine recognition signal in the C-terminal portion of the tyrosinase molecule. In the AP-3-deficient cells, tyrosinase was also present in structures resembling late endosomes or multivesicular bodies; these vesicles contained exvaginations devoid of tyrosinase. This suggests that, under normal circumstances, AP-3 may act on multivesicular bodies to form tyrosinase-containing vesicles destined to fuse with premelanosomes. Finally, our studies demonstrate that tyrosinase and TRP-1 usedifferent mechanisms to reach their premelanosomal destination.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 12:49:11