Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Cytoplasmic tail motifs mediate endoplasmic reticulum localization and export of transmembrane reporters in the protozoan parasite Toxoplasma gondii
Autore:
Hoppe, HC; Joiner, KA;
Indirizzi:
Yale Univ, Sch Med, Dept Internal Med, Infect Dis Sect, New Haven, CT 06520 USA Yale Univ New Haven CT USA 06520 Infect Dis Sect, New Haven, CT 06520 USA
Titolo Testata:
CELLULAR MICROBIOLOGY
fascicolo: 6, volume: 2, anno: 2000,
pagine: 569 - 578
SICI:
1462-5814(200012)2:6<569:CTMMER>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
STOMATITIS-VIRUS GLYCOPROTEIN; TYROSINE-CONTAINING MOTIF; TRANS-GOLGI NETWORK; SECRETORY PATHWAY; MEMBRANE-PROTEINS; BREFELDIN-A; MDCK CELLS; HELA-CELLS; ER; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Joiner, KA Yale Univ, Sch Med, Dept Internal Med, Infect Dis Sect, 333 Cedar St, New Haven, CT 06520 USA Yale Univ 333 Cedar St New Haven CT USA 06520 ven, CT 06520 USA
Citazione:
H.C. Hoppe e K.A. Joiner, "Cytoplasmic tail motifs mediate endoplasmic reticulum localization and export of transmembrane reporters in the protozoan parasite Toxoplasma gondii", CELL MICROB, 2(6), 2000, pp. 569-578

Abstract

In mammalian cells and yeasts, amino acid motifs in the cytoplasmic tails of transmembrane proteins play a prominent role in protein targeting in theearly secretory pathway by mediating localization to or rapid export from the endoplasmic reticulum (ER). However, early sorting events are poorly characterized in protozoan parasites. Here, we show that a C-terminal QKTT sequence mediates the ER localization of chimeric reporter constructs consisting of bacterial alkaline phosphatase (BAP) fused to the transmembrane domain (TMD) and truncated cytoplasmic tail of the human low-density lipoprotein receptor (LDL) receptor or of murine lysosome-associated membrane protein(lamp-1) in Toxoplasma gondii. The cytoplasmic tail of human TGN46 also determines ER localization of BAP chimeras in the parasite, but this can be overcome by the addition at the C-terminus of the tail of an acidic patch, which functions as an ER export signal in conjunction with an upstream tyrosine motif. These results suggest that COPI-dependent ER retrieval and COPII-dependent export mechanisms mediated by KKXX and DXE motifs of mammalian cells are generally conserved in T. gondii, In contrast, the failure of the QKTT motif and TGN46 cytoplasmic tail to induce steady-state ER localization of vesicular stomatitis virus glycoprotein (VSVG) chimeras in HeLa and NRK cells indicates that significant differences in early secretory trafficking also exist.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 19:20:07