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PMID:21229326

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Citation

Zhang, Y, Zhou, X, Zhao, L, Li, C, Zhu, H, Xu, L, Shan, L, Liao, X, Guo, Z and Huang, P (2011) UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2. Mol. Cells 31:113-22

Abstract

Fanconi anemia (FA) is a rare cancer-predisposing genetic disease mostly caused by improper regulation of the monoubiquitination of Fanconi anemia complementation group D2 (FANCD2). Genetic studies have indicated that ubiquitin conjugating enzyme UBE2T and HHR6 could regulate FANCD2 monoubiquitination through distinct mechanisms. However, the exact regulation mechanisms of FANCD2 monoubiquitination in response to different DNA damages remain unclear. Here we report that UBE2W, a new ubiquitin conjugating enzyme, could regulate FANCD2 monoubiquitination by mechanisms different from UBE2T or HHR6. Indeed, UBE2W exhibits ubiquitin conjugating enzyme activity and catalyzes the monoubiquitination of PHD domain of Fanconi anemia complementation group L (FANCL) in vitro. UBE2W binds to FANCL, and the PHD domain is both necessary and sufficient for this interaction in mammalian cells. In addition, over-expression of UBE2W in cells promotes the monoubiquitination of FANCD2 and down-regulated UBE2W markedly reduces the UV irradiation-induced but not MMC-induced FANCD2 monoubiquitination. These results indicate that UBE2W regulates FANCD2 monoubiquitination by mechanisms different from UBE2T and HRR6. It may provide an additional regulatory step in the activation of the FA pathway.

Links

PubMed Online version:10.1007/s10059-011-0015-9

Keywords

Amino Acid Sequence; Animals; Cell Nucleus/drug effects; Cell Nucleus/metabolism; Cell Nucleus/radiation effects; Fanconi Anemia Complementation Group D2 Protein/metabolism; Fanconi Anemia Complementation Group L Protein/chemistry; Fanconi Anemia Complementation Group L Protein/metabolism; HeLa Cells; Humans; Mice; Mitomycin/pharmacology; Molecular Sequence Data; NIH 3T3 Cells; Protein Binding/drug effects; Protein Binding/radiation effects; Protein Structure, Tertiary; Saccharomyces cerevisiae/cytology; Saccharomyces cerevisiae/metabolism; Ubiquitin-Conjugating Enzymes/chemistry; Ubiquitin-Conjugating Enzymes/metabolism; Ubiquitination/drug effects; Ubiquitination/radiation effects; Ultraviolet Rays

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

MOUSE:UBE2W

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9CR14

F

Seeded From UniProt

complete

MOUSE:UBE2W

located_in

GO:0005634: nucleus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

MOUSE:UBE2W

involved_in

GO:0006513: protein monoubiquitination

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:UBE2W

enables

GO:0004842: ubiquitin-protein transferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

MOUSE:UBE2W

enables

GO:0061631: ubiquitin conjugating enzyme activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:UBE2W

involved_in

GO:0006513: protein monoubiquitination

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:UBE2W

enables

GO:0004842: ubiquitin-protein transferase activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

MOUSE:FANCL

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8VDW4

F

Seeded From UniProt

complete

MOUSE:FANCL

enables

GO:0004842: ubiquitin-protein transferase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

MOUSE:FANCL

enables

GO:0061630: ubiquitin protein ligase activity

ECO:0000314: direct assay evidence used in manual assertion

F

  • has_input:(MGI:MGI:2448480)

Seeded From UniProt

complete


See also

References

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