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The cation-π interaction in cysteine-rich domain of Smoothened is critical for its cholesterylation and function

التفاصيل البيبلوغرافية
العنوان: The cation-π interaction in cysteine-rich domain of Smoothened is critical for its cholesterylation and function
المؤلفون: Kong Zekai, Xu Min, Zhang Yanqing, Huang Wenda, Zhao Xiaolu, Luo Jie, Song Bao-Liang
المصدر: Acta Biochimica et Biophysica Sinica, Vol 54, Pp 1171-1179 (2022)
بيانات النشر: China Science Publishing & Media Ltd., 2022.
سنة النشر: 2022
المجموعة: LCC:Biochemistry
LCC:Genetics
مصطلحات موضوعية: Hedgehog, Smoothened, cholesterylation, cysteine-rich domain, cation-π interaction, Biochemistry, QD415-436, Genetics, QH426-470
الوصف: The Hedgehog (Hh) signaling pathway is critical for embryonic development and tissue renewal. The G protein-coupled receptor (GPCR)-like protein Smoothened (SMO) is the central signal transducer in the Hh pathway. Cholesterol binds and then covalently links to the D95 residue of cysteine-rich domain (CRD) of human SMO. The cholesterylation of CRD is critical for SMO activation. SMO cholesterylation is a Ca2+-boosted autoreaction that requires the formation of an ester bond between the side chains of D95 and Y130 as an intermediate. It is unknown whether other residues of SMO are involved in the esterification between D95 and cholesterol. In this study, we find that the SMO-CRD(27–192) can undergo cholesterylation. In addition to D95 and Y130, the residues critical for cholesterol modification include Y85, T88, T90, W109, W119, K133, E160 and F166. T88, W109, W119 and F166 also seem to be involved in protein folding. Notably, we find that Y85 and K133 form a cation-π interaction whose disruption abolishes cholesterylation and ciliary localization of SMO. This study highlights the mechanism and function of cholesterol modification of SMO.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1672-9145
العلاقة: https://doaj.org/toc/1672-9145Test
DOI: 10.3724/abbs.2022090
الوصول الحر: https://doaj.org/article/660dcb41b21b49408130585871a1d84fTest
رقم الانضمام: edsdoj.660dcb41b21b49408130585871a1d84f
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:16729145
DOI:10.3724/abbs.2022090