Induced degradation of SNAP-fusion proteins†

IF 4.2 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY RSC Chemical Biology Pub Date : 2024-10-21 DOI:10.1039/D4CB00184B
Savina Abraham Pol, Sara Liljenberg, Jack Barr, Gina Simon, Luis Wong-Dilworth, Danielle L. Paterson, Vladimir P. Berishvili, Francesca Bottanelli, Farnusch Kaschani, Markus Kaiser, Mariell Pettersson and Doris Hellerschmied
{"title":"Induced degradation of SNAP-fusion proteins†","authors":"Savina Abraham Pol, Sara Liljenberg, Jack Barr, Gina Simon, Luis Wong-Dilworth, Danielle L. Paterson, Vladimir P. Berishvili, Francesca Bottanelli, Farnusch Kaschani, Markus Kaiser, Mariell Pettersson and Doris Hellerschmied","doi":"10.1039/D4CB00184B","DOIUrl":null,"url":null,"abstract":"<p >Self-labeling protein tags are an efficient means to visualize, manipulate, and isolate engineered fusion proteins with suitable chemical probes. The SNAP-tag, which covalently conjugates to benzyl–guanine and –chloropyrimidine derivatives is used extensively in fluorescence microscopy, given the availability of suitable SNAP-ligand-based probes. Here, we extend the applicability of the SNAP-tag to targeted protein degradation. We developed a set of SNAP PROteolysis TArgeting Chimeras (SNAP-PROTACs), which recruit the VHL or CRBN-ubiquitin E3 ligases to induce the degradation of SNAP-fusion proteins. Endogenous tagging enabled the visualization and the selective depletion of a SNAP-clathrin light chain fusion protein using SNAP-PROTACs. The addition of PROTACs to the SNAP-tag reagent toolbox facilitates the comprehensive analysis of protein function with a single gene tagging event.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" 12","pages":" 1232-1247"},"PeriodicalIF":4.2000,"publicationDate":"2024-10-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11494418/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"RSC Chemical Biology","FirstCategoryId":"1085","ListUrlMain":"https://pubs.rsc.org/en/content/articlelanding/2024/cb/d4cb00184b","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Self-labeling protein tags are an efficient means to visualize, manipulate, and isolate engineered fusion proteins with suitable chemical probes. The SNAP-tag, which covalently conjugates to benzyl–guanine and –chloropyrimidine derivatives is used extensively in fluorescence microscopy, given the availability of suitable SNAP-ligand-based probes. Here, we extend the applicability of the SNAP-tag to targeted protein degradation. We developed a set of SNAP PROteolysis TArgeting Chimeras (SNAP-PROTACs), which recruit the VHL or CRBN-ubiquitin E3 ligases to induce the degradation of SNAP-fusion proteins. Endogenous tagging enabled the visualization and the selective depletion of a SNAP-clathrin light chain fusion protein using SNAP-PROTACs. The addition of PROTACs to the SNAP-tag reagent toolbox facilitates the comprehensive analysis of protein function with a single gene tagging event.

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
诱导 SNAP 融合蛋白降解。
自标记蛋白质标签是利用合适的化学探针观察、操作和分离工程融合蛋白的有效方法。SNAP 标签能与苄基鸟嘌呤和氯嘧啶衍生物共价结合,由于有合适的基于 SNAP 配体的探针,它在荧光显微镜中得到了广泛应用。在这里,我们将 SNAP 标记的适用性扩展到靶向蛋白质降解。我们开发了一组 SNAP PROteolysis TArgeting Chimeras(SNAP-PROTACs),它们能招募 VHL 或 CRBN-ubiquitin E3 连接酶来诱导 SNAP 融合蛋白的降解。使用 SNAP-PROTACs 对 SNAP-clathrin 轻链融合蛋白进行内源标记可实现可视化和选择性降解。在 SNAP 标记试剂工具箱中加入 PROTACs 后,只需一次基因标记就能对蛋白质功能进行全面分析。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
CiteScore
6.10
自引率
0.00%
发文量
128
审稿时长
10 weeks
期刊最新文献
Back cover Cultivating the future leaders of chemical biology. Rational engineering of an antimalarial peptide with enhanced proteolytic stability and preserved parasite invasion inhibitory activity. A nanoengineered tandem nitroreductase: designing a robust prodrug-activating nanoreactor. A platform of ADAPTive scaffolds: development of CDR-H3 β-hairpin mimics into covalent inhibitors of the PD1/PDL1 immune checkpoint†
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1