دورية أكاديمية
أعرض في EDS

SENP8 limits aberrant neddylation of NEDD8 pathway components to promote cullin-RING ubiquitin ligase function.

التفاصيل البيبلوغرافية
العنوان: SENP8 limits aberrant neddylation of NEDD8 pathway components to promote cullin-RING ubiquitin ligase function.
المؤلفون: Coleman KE; Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States., Békés M; Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States., Chapman JR; Proteomics Laboratory, Division of Advanced Research Technologies, New York University School of Medicine, New York, United States., Crist SB; Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States., Jones MJ; Molecular Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, Unites States., Ueberheide BM; Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States.; Proteomics Laboratory, Division of Advanced Research Technologies, New York University School of Medicine, New York, United States., Huang TT; Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, United States.
المصدر: ELife [Elife] 2017 May 05; Vol. 6. Date of Electronic Publication: 2017 May 05.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: Protein Processing, Post-Translational*, Endopeptidases/*metabolism , NEDD8 Protein/*metabolism , Ubiquitin-Conjugating Enzymes/*metabolism, Cell Cycle ; Gene Expression Regulation ; HEK293 Cells ; HeLa Cells ; Humans
مستخلص: NEDD8 is a ubiquitin-like modifier most well-studied for its role in activating the largest family of ubiquitin E3 ligases, the cullin-RING ligases (CRLs). While many non-cullin neddylation substrates have been proposed over the years, validation of true NEDD8 targets has been challenging, as overexpression of exogenous NEDD8 can trigger NEDD8 conjugation through the ubiquitylation machinery. Here, we developed a deconjugation-resistant form of NEDD8 to stabilize the neddylated form of cullins and other non-cullin substrates. Using this strategy, we identified Ubc12, a NEDD8-specific E2 conjugating enzyme, as a substrate for auto-neddylation. Furthermore, we characterized SENP8/DEN1 as the protease that counteracts Ubc12 auto-neddylation, and observed aberrant neddylation of Ubc12 and other NEDD8 conjugation pathway components in SENP8-deficient cells. Importantly, loss of SENP8 function contributes to accumulation of CRL substrates and defective cell cycle progression. Thus, our study highlights the importance of SENP8 in maintaining proper neddylation levels for CRL-dependent proteostasis.
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معلومات مُعتمدة: F32 GM100598 United States GM NIGMS NIH HHS; P30 CA016087 United States CA NCI NIH HHS; R01 ES025166 United States ES NIEHS NIH HHS
فهرسة مساهمة: Keywords: CRL; Nedd8; Ubc12; Ubl protease; biochemistry; human; ubiquitin
المشرفين على المادة: 0 (NEDD8 Protein)
0 (NEDD8 protein, human)
EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes)
EC 3.4.- (Endopeptidases)
EC 3.4.22.- (SENP8 protein, human)
EC 6.3.2.- (UBE2M protein, human)
تواريخ الأحداث: Date Created: 20170506 Date Completed: 20180205 Latest Revision: 20240531
رمز التحديث: 20240531
مُعرف محوري في PubMed: PMC5419743
DOI: 10.7554/eLife.24325
PMID: 28475037
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.24325