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Titolo:
Ubc9 interacts with a nuclear localization signal and mediates nuclear localization of the paired-like homeobox protein Vsx-1 independent of SUMO-1 modification
Autore:
Kurtzman, AL; Schechter, N;
Indirizzi:
SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA SUNYStony Brook Stony Brook NY USA 11794 Biol, Stony Brook, NY 11794 USA SUNY Stony Brook, Dept Psychiat & Behav Sci, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Sci, Stony Brook, NY 11794 USA SUNY Stony Brook, Inst Cell & Dev Biol, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Biol, Stony Brook, NY 11794 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 10, volume: 98, anno: 2001,
pagine: 5602 - 5607
SICI:
0027-8424(20010508)98:10<5602:UIWANL>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
UBIQUITIN-CONJUGATING ENZYME; VERTEBRATE EYE DEVELOPMENT; GTPASE-ACTIVATING PROTEIN; ADULT GOLDFISH RETINA; COVALENT MODIFICATION; TRANSCRIPTION FACTOR; PORE COMPLEX; 2-HYBRID SYSTEM; GENE; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Schechter, N SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 rook, NY 11794 USA
Citazione:
A.L. Kurtzman e N. Schechter, "Ubc9 interacts with a nuclear localization signal and mediates nuclear localization of the paired-like homeobox protein Vsx-1 independent of SUMO-1 modification", P NAS US, 98(10), 2001, pp. 5602-5607

Abstract

Vsx-1 is a paired-like:CVC homeobox gene whose expression is linked to bipolar cell differentiation during zebrafish retinogenesis. We used a yeast two-hybrid screen to identify proteins interacting with Vsx-1 and isolated Ubc9, an enzyme that conjugates the small ubiquitin-like modifier SUMO-1, Despite its interaction with Ubc9, we show that Vsx-1 is not a substrate for SUMO-1 in COS-7 cells or in vitro, When a yeast two-hybrid assay is used. deletion analysis of the interacting domain on Vsx-1 shows that Ubc9 binds to a nuclear localization signal (NLS) at the NH2 terminus of the homeodomain, In SW13 cells, Vsx-1 localizes to the nucleus and is excluded from nucleoli. Deletion of the NLS disrupts this nuclear localization, resulting in adiffuse cytoplasmic distribution of Vsx-1. In SW13 AK1 cells that express low levels of endogenous Ubc9, Vsx-1 accumulates in a perinuclear ring and colocalizes with an endoplasmic reticulum marker. However, NLS-tagged STAT1protein exhibits normal nuclear localization in both SW13 and SW13 AK1 cells, suggesting that nuclear import is not globally disrupted. Cotransfection of Vsx-1 with Ubc9 restores Vsx-1 nuclear localization in SW3 AK1 cells and demonstrates that Ubc9 is required for the nuclear localization of Vsx-1. Ubc9 continues to restore nuclear localization even after a C935 active site mutation has eliminated its SUMO-1-conjugating ability. These results suggest that Ubc9 mediates the nuclear localization of Vsx-1, and possibly other proteins, through a nonenzymatic mechanism that is independent of SUMO-1 conjugation,

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 16:59:00