دورية أكاديمية
أعرض في EDS

Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family.

التفاصيل البيبلوغرافية
العنوان: Redefining the catalytic HECT domain boundaries for the HECT E3 ubiquitin ligase family.
المؤلفون: Kane EI; Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, U.S.A., Beasley SA; Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, U.S.A., Schafer JM; Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, U.S.A., Bohl JE; Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, U.S.A., Lee YS; Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, U.S.A., Rich KJ; Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, U.S.A., Bosia EF; Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, U.S.A., Spratt DE; Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, U.S.A.
المصدر: Bioscience reports [Biosci Rep] 2022 Oct 28; Vol. 42 (10).
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 8102797 Publication Model: Print Cited Medium: Internet ISSN: 1573-4935 (Electronic) Linking ISSN: 01448463 NLM ISO Abbreviation: Biosci Rep Subsets: MEDLINE
أسماء مطبوعة: Publication: London : Portland Press on behalf of the Biochemical Society
Original Publication: London : The Biochemical Society, c1981-
مواضيع طبية MeSH: Ubiquitin-Protein Ligases*/metabolism , Ubiquitins*/metabolism, Catalytic Domain ; Humans ; Ubiquitination
مستخلص: There are 28 unique human members of the homologous to E6AP C-terminus (HECT) E3 ubiquitin ligase family. Each member of the HECT E3 ubiquitin ligases contains a conserved bilobal HECT domain of approximately 350 residues found near their C-termini that is responsible for their respective ubiquitylation activities. Recent studies have begun to elucidate specific roles that each HECT E3 ubiquitin ligase has in various cancers, age-induced neurodegeneration, and neurological disorders. New structural models have been recently released for some of the HECT E3 ubiquitin ligases, but many HECT domain structures have yet to be examined due to chronic insolubility and/or protein folding issues. Building on these recently published structural studies coupled with our in-house experiments discussed in the present study, we suggest that the addition of ∼50 conserved residues preceding the N-terminal to the current UniProt defined boundaries of the HECT domain are required for isolating soluble, stable, and active HECT domains. We show using in silico bioinformatic analyses coupled with secondary structural prediction software that this predicted N-terminal α-helix found in all 28 human HECT E3 ubiquitin ligases forms an obligate amphipathic α-helix that binds to a hydrophobic pocket found within the HECT N-terminal lobe. The present study brings forth the proposal to redefine the residue boundaries of the HECT domain to include this N-terminal extension that will likely be critical for future biochemical, structural, and therapeutic studies on the HECT E3 ubiquitin ligase family.
(© 2022 The Author(s).)
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معلومات مُعتمدة: R15 GM126432 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: HECT E3 ubiquitin ligase; HECT domain; UniProt; multiple sequence alignment; ubiquitin; ubiquitylation
المشرفين على المادة: 0 (Ubiquitins)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
تواريخ الأحداث: Date Created: 20220916 Date Completed: 20221005 Latest Revision: 20231102
رمز التحديث: 20240829
مُعرف محوري في PubMed: PMC9547173
DOI: 10.1042/BSR20221036
PMID: 36111624
قاعدة البيانات: MEDLINE
الوصف
تدمد:1573-4935
DOI:10.1042/BSR20221036