DSSylation, a novel guide for protein degradation?

References

[1] BondaDJ, WangX, PerryG, NunomuraA, TabatonM, ZhuX, SmithMA (2010) Oxidative stress in Alzheimer disease: a possibility for prevention. Neuropharmacology59: 290-294

[2] CrackowerMA, SchererSW, RommensJM, HuiC-C, PoorkajP, SoderS, CobbenJM, HudginsL, EvansJP, TsuiL-C (1996) Characterization of the split hand/split foot malformation locus SHFM1 at 7q21. 3-q22. 1 and analysis of a candidate gene for its expression during limb development. Hum Mol Genet5: 571-579

[3] FunakoshiM, LiX, VelichutinaI, HochstrasserM, KobayashiH (2004) Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability. J Cell Sci117: 6447-6454

[4] HauserDN, HastingsTG (2012) Mitochondrial dysfunction and oxidative stress in Parkinson’s disease and monogenic parkinsonism. Neurobiol Dis51: 35-42

[5] KojicM, YangH, KostrubCF, PavletichNP, HollomanWK (2003) The BRCA2-interacting protein DSS1 is vital for DNA repair, recombination, and genome stability in Ustilago maydis. Mol Cell12: 1043-1049

[6] MarstonNJ, RichardsWJ, HughesD, BertwistleD, MarshallCJ, AshworthA (1999) Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals. Mol Cell Biol19: 4633-4642

[7] MenziesFM, MoreauK, RubinszteinDC (2011) Protein misfolding disorders and macroautophagy. Curr Opin Cell Biol23: 190-197

[8] QinS, WangQ, RayA, WaniG, ZhaoQ, BhaumikSR, WaniAA (2009) Sem1p and Ubp6p orchestrate telomeric silencing by modulating histone H2B ubiquitination and H3 acetylation. Nucleic Acids Res37: 1843-1853

[9] SoneT, SaekiY, Toh-eA, YokosawaH (2004) Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae. J Biol Chem279: 28807-28816

[10] ThakurtaAG, GopalG, YoonJH, KozakL, DharR (2005) Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p for mRNA export in fission yeast. EMBO J24: 2512-2523

[11] WeiS-J, TrempusCS, CannonRE, BortnerCD, TennantRW (2003) Identification of Dss1 as a 12-O-tetradecanoylphorbol-13-acetate-responsive gene expressed in keratinocyte progenitor cells, with possible involvement in early skin tumorigenesis. J Biol Chem278: 1758-1768

[12] WeiS-J, WilliamsJG, DangH, DardenTA, BetzBL, HumbleMM, ChangF-M, TrempusCS, JohnsonK, CannonRE (2008) Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation. J Mol Biol383: 693-712

[13] WilmesGM, BergkesselM, BandyopadhyayS, ShalesM, BrabergH, CagneyG, CollinsSR, WhitworthGB, KressTL, WeissmanJS (2008) A genetic interaction map of RNA-processing factors reveals links between Sem1/Dss1-containing complexes and mRNA export and splicing. Mol Cell32: 735-746

[14] YangH, JeffreyPD, MillerJ, KinnucanE, SunY, ThomäNH, ZhengN, ChenP-L, LeeW-H, PavletichNP (2002) BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure. Science297: 1837-1848

[15] ZhangY, ChangF-M, HuangJ, JuncoJJ, MaffiSK, PridgenHI, CatanoG, DangH, DingX, YangF, KimDJ, SlagaTJ, HeR, WeiS-J (2014) DSSylation, a novel protein modification targets proteins induced by oxidative stress, and facilitates their degradation in cells. Prot Cell.

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