SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein

Endter, Christian and Kzhyshkowska, Julia and Stauber, Roland and Dobner, Thomas (2001) SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 98 (20). pp. 11312-11317. ISSN 0027-8424

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Abstract

SUMO-1 is a small ubiquitin-related modifier protein that is covalently linked to many cellular and viral protein targets. Modification by SUMO-1 is proposed to play a role in protein targeting and/or stability. We show here that adenovirus type 5 early region 1B 55-kDa (E1B-55kDa) oncoprotein can be covalently modified by SUMO-1 in vivo through a major attachment site comprising a single lysine residue at amino acid position 104. The sequence surrounding this lysine matches the proposed psi KxE consensus motif required for SUMO-1 conjugation. A single mutation (K104R) that abolishes SUMOylation of E1B-55kDa dramatically reduces the ability of the adenovirus type 5 protein to transform primary baby rat kidney cells in cooperation with E1A and to inhibit p53-mediated transactivation. Overexpression of SUMO-1 in adenovirus type 5E1A/E1B-55kDa-transformed baby rat kidney cells causes the relocalization of E1B-55kDa from the cytoplasm to the nucleus, where it accumulates with SUMO-1 in dot- or track-like structures. Significantly, when SUMO-1 is ectopically expressed in transformed rat cells no effect on the cytoplasmic localization of the E1B-K104R mutant protein is observed. Our results demonstrate that SUMO-1 modification is required for transformation by adenovirus type 5E1B-55kDa and provide further evidence for the idea that this posttranslational modification plays a role in protein targeting to specific subcellular sites.

Item Type: Article
Uncontrolled Keywords: E1B-58KD TUMOR-ANTIGEN; TRANSCRIPTIONAL REPRESSION; 55-KILODALTON ONCOPROTEIN; P53-DEPENDENT APOPTOSIS; CELLULAR PROTEIN; P53 ACETYLATION; E4ORF6 PROTEIN; E1B PROTEIN; CELLS; PML;
Subjects: 600 Technology > 610 Medical sciences Medicine
Divisions: Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene
Depositing User: Dr. Gernot Deinzer
Date Deposited: 07 Dec 2021 07:30
Last Modified: 07 Dec 2021 07:30
URI: https://pred.uni-regensburg.de/id/eprint/41094

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