诱导 SNAP 融合蛋白降解。

IF 4.2 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
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":"诱导 SNAP 融合蛋白降解。","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":"{\"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}","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

摘要

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。

Induced degradation of SNAP-fusion proteins†

Induced degradation of SNAP-fusion proteins†

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.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 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
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信