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Titolo:
PROTEIN SORTING BY TYROSINE-BASED SIGNALS - ADAPTING TO THE YS AND WHEREFORES
Autore:
MARKS MS; OHNO H; KIRCHHAUSEN T; BONIFACINO SJ;
Indirizzi:
UNIV PENN,SCH MED,DEPT PATHOL & LAB MED PHILADELPHIA PA 19104 NICHHD,CELL BIOL & METAB BRANCH,NIH BETHESDA MD 20892 HARVARD UNIV,SCH MED,DEPT CELL BIOL BOSTON MA 02115 CTR BLOOD RES BOSTON MA 02115
Titolo Testata:
Trends in cell biology
fascicolo: 3, volume: 7, anno: 1997,
pagine: 124 - 128
SICI:
0962-8924(1997)7:3<124:PSBTS->2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
LYSOSOMAL ACID-PHOSPHATASE; TRANS-GOLGI NETWORK; ENDOCYTIC PATHWAY; CYTOPLASMIC TAIL; PLASMA-MEMBRANE; CELL-SURFACE; COATED VESICLES; ASIALOGLYCOPROTEIN RECEPTOR; INTERNALIZATION SIGNAL; INVITRO BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
M.S. Marks et al., "PROTEIN SORTING BY TYROSINE-BASED SIGNALS - ADAPTING TO THE YS AND WHEREFORES", Trends in cell biology, 7(3), 1997, pp. 124-128

Abstract

The endocytic and secretory pathways of eukaryotic cells consist of an away of membrane-bound compartments, each of which contains a characteristic cohort of transmembrane proteins. Understanding how these proteins are targeted to and maintained within their appropriate compartments will be crucial for unravelling the mysteries of organelle biogenesis and function. A common event in the sorting of many transmembraneproteins is the interaction between a sorting signal in the cytosolicdomain of the targeted protein and a component of an organellar protein coat. Here, we summarize recent findings on the mechanism of sorting by one type of signal, characterized by the presence of a critical tyrosine (Y) residue, and attempt to integrate these findings into a hypothetical model for protein sorting in the endocytic and late (post-Golgi) secretory pathways.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 20:28:11