» Articles » PMID: 16758298

Role of SUMO/Ubc9 in DNA Damage Repair and Tumorigenesis

Overview
Journal J Mol Histol
Specialty Biochemistry
Date 2006 Jun 8
PMID 16758298
Citations 16
Authors
Affiliations
Soon will be listed here.
Abstract

DNA damage repair is an important cell function for genome integrity and its deregulation can lead to genomic instability and development of malignancies. Sumoylation is an increasingly important ubiquitin-like modification of proteins affecting protein stability, enzymatic activity, nucleocytoplasmic trafficking, and protein-protein interactions. In particular, several important DNA repair enzymes are subject to sumoylation, which appears to play a role in copping with DNA damage insults. Recent reports indicate that Ubc9, the single SUMO E2 enzyme catalyzing the conjugation of SUMO to target proteins, is overexpressed in certain tumors, such as lung adenocarcinoma, ovarian carcinoma and melanoma, suggestive of its clinic significance. This review summarizes the most important DNA damage repair pathways which are potentially affected by Ubc9/SUMO and their role in regulating the function of several proteins involved in the DNA damage repair machinery.

Citing Articles

Repression of the SUMO-conjugating enzyme UBC9 is associated with lowered double minutes and reduced tumor progression.

Wang Y, Zou H, Ji W, Huang M, You B, Sun N Cancer Biol Ther. 2024; 25(1):2323768.

PMID: 38465861 PMC: 10936631. DOI: 10.1080/15384047.2024.2323768.


An Update on the Role of Ubiquitination in Melanoma Development and Therapies.

Soysouvanh F, Giuliano S, Habel N, El-Hachem N, Pisibon C, Bertolotto C J Clin Med. 2021; 10(5).

PMID: 33800394 PMC: 7962844. DOI: 10.3390/jcm10051133.


Functional Analysis of the Replication Fork Proteome Identifies BET Proteins as PCNA Regulators.

Wessel S, Mohni K, Luzwick J, Dungrawala H, Cortez D Cell Rep. 2019; 28(13):3497-3509.e4.

PMID: 31553917 PMC: 6878991. DOI: 10.1016/j.celrep.2019.08.051.


Variation in expression of small ubiquitin-like modifiers in injured sciatic nerve of mice.

Zhang D, Yu K, Yang Z, Liu X, Ma X, Li Y Neural Regen Res. 2019; 14(8):1455-1461.

PMID: 30964073 PMC: 6524499. DOI: 10.4103/1673-5374.253531.


Inhibition of the Ubc9 E2 SUMO-conjugating enzyme-CRMP2 interaction decreases NaV1.7 currents and reverses experimental neuropathic pain.

Francois-Moutal L, Dustrude E, Wang Y, Brustovetsky T, Dorame A, Ju W Pain. 2018; 159(10):2115-2127.

PMID: 29847471 PMC: 6150792. DOI: 10.1097/j.pain.0000000000001294.


References
1.
Weger S, Hammer E, Heilbronn R . Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo. FEBS Lett. 2005; 579(22):5007-12. DOI: 10.1016/j.febslet.2005.07.088. View

2.
Romanenko A, Kinoshita A, Wanibuchi H, Wei M, Zaparin W, Vinnichenko W . Involvement of ubiquitination and sumoylation in bladder lesions induced by persistent long-term low dose ionizing radiation in humans. J Urol. 2006; 175(2):739-43. DOI: 10.1016/S0022-5347(05)00172-2. View

3.
Chen L, Chen J . MDM2-ARF complex regulates p53 sumoylation. Oncogene. 2003; 22(34):5348-57. DOI: 10.1038/sj.onc.1206851. View

4.
Isik S, Sano K, Tsutsui K, Seki M, Enomoto T, Saitoh H . The SUMO pathway is required for selective degradation of DNA topoisomerase IIbeta induced by a catalytic inhibitor ICRF-193(1). FEBS Lett. 2003; 546(2-3):374-8. DOI: 10.1016/s0014-5793(03)00637-9. View

5.
Seufert W, Futcher B, Jentsch S . Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature. 1995; 373(6509):78-81. DOI: 10.1038/373078a0. View