Discover bacteria最新文献

筛选
英文 中文
Enzymatic versatility of the salmonella effector SopB enables manipulation of host phosphoinositide signalling. 沙门氏菌效应物SopB酶的多功能性使操纵宿主磷酸肌苷信号传导成为可能。
Discover bacteria Pub Date : 2026-01-01 Epub Date: 2026-08-22 DOI: 10.1007/s44351-026-00056-8
Ronan C Jensen, Gregory D Fairn
{"title":"Enzymatic versatility of the salmonella effector SopB enables manipulation of host phosphoinositide signalling.","authors":"Ronan C Jensen, Gregory D Fairn","doi":"10.1007/s44351-026-00056-8","DOIUrl":"10.1007/s44351-026-00056-8","url":null,"abstract":"<p><p><i>Salmonella enterica</i> relies on type III secreted effector proteins to invade host cells and establish an intracellular replicative niche, the <i>Salmonella</i>-containing vacuole (SCV). Among these effectors, SopB (also known as SigD) is notable for its functional versatility, contributing to virtually every stage of infection. Long characterized as a phosphoinositide phosphatase and inositol polyphosphate phosphatase, SopB was recently shown to also possess phosphotransferase activity, generating PtdIns(3,4)P<sub>2</sub> (and, transiently, PtdIns(3,4,5)P<sub>3</sub>) <i>de novo</i> from PtdIns(4,5)P<sub>2</sub> independently of PI 3-kinases and ATP. This discovery reframes how SopB activates the pro-survival kinase Akt and manipulates host signalling during invasion. Beyond its enzymatic activities, SopB engages the host Rho GTPases Cdc42 through a structurally distinct N-terminal domain and reorganizes the vimentin intermediate filament network to stabilize the SCV. In this review, we consider SopB as a paradigm for multifunctional effector biology, integrating its dual enzymatic activities, vimentin manipulation, anti-apoptotic signalling, and post-translational regulation into a unified model of how a single bacterial protein rewires host phosphoinositide metabolism across space and time.</p>","PeriodicalId":524180,"journal":{"name":"Discover bacteria","volume":"3 1","pages":"19"},"PeriodicalIF":0.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540636/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148890177","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
0
×
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×
相关产品
×
本文献相关产品
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:604180095
Book学术官方微信
小红书