一項對細(xì)胞復(fù)雜組成的驚人發(fā)現(xiàn)可能導(dǎo)致開發(fā)新型藥物,。
研究細(xì)胞蛋白質(zhì)間相互作用的研究人員發(fā)現(xiàn),蛋白質(zhì)間的通訊不是通過一系列簡單的一對一通訊,,而是通過一個復(fù)雜的化學(xué)信號網(wǎng)絡(luò),。
研究結(jié)果表明,如果采取不同設(shè)計,,藥物將會更為有效,。藥物將針對發(fā)揮作用的一組蛋白質(zhì),而非單個蛋白質(zhì),。
這項研究結(jié)果是在研究酵母細(xì)胞中獲得的,,酵母細(xì)胞中存在多種與人體細(xì)胞相關(guān)的蛋白質(zhì)。研究人員使用先進(jìn)技術(shù)甄別出數(shù)以百計的不同蛋白質(zhì),,然后使用統(tǒng)計學(xué)分析找出這些蛋白質(zhì)間隔為重要的鏈接,,一共繪出幾乎2000個聯(lián)結(jié)。
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研究人員期望發(fā)現(xiàn)單個蛋白質(zhì)間的簡單聯(lián)系,,但卻意外發(fā)現(xiàn)這些蛋白質(zhì)連接成一個復(fù)雜的網(wǎng)絡(luò),。
參與這項研究的愛丁堡大學(xué)Victor Neduva博士表示:“這項研究發(fā)現(xiàn)一個錯綜復(fù)雜的細(xì)胞內(nèi)蛋白質(zhì)網(wǎng)絡(luò),遠(yuǎn)比之前想象的復(fù)雜,。這些表明,,藥物應(yīng)該更為復(fù)雜,,才可以更為有效地治療疾病。”領(lǐng)導(dǎo)這項研究的Mike Tyers教授指出,,“如果藥物針對與某種疾病有關(guān)的蛋白質(zhì)網(wǎng)絡(luò)而非只針對單獨(dú)一種蛋白質(zhì),,效果應(yīng)該會更好。”(生物谷Bioon.net)
生物谷推薦原文出處:
Science DOI: 10.1126/science.1176495
A Global Protein Kinase and Phosphatase Interaction Network in Yeast
Ashton Breitkreutz,1,* Hyungwon Choi,2,* Jeffrey R. Sharom,1,3,* Lorrie Boucher,1,* Victor Neduva,4,* Brett Larsen,1 Zhen-Yuan Lin,1 Bobby-Joe Breitkreutz,1 Chris Stark,1 Guomin Liu,1 Jessica Ahn,1 Danielle Dewar-Darch,1 Teresa Reguly,1 Xiaojing Tang,1 Ricardo Almeida,4 Zhaohui Steve Qin,5 Tony Pawson,1,3 Anne-Claude Gingras,1,3, Alexey I. Nesvizhskii,2,6, Mike Tyers1,3,4,
The interactions of protein kinases and phosphatases with their regulatory subunits and substrates underpin cellular regulation. We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes. The KPI network contained many dense local regions of interactions that suggested new functions. Notably, the cell cycle phosphatase Cdc14 associated with multiple kinases that revealed roles for Cdc14 in mitogen-activated protein kinase signaling, the DNA damage response, and metabolism, whereas interactions of the target of rapamycin complex 1 (TORC1) uncovered new effector kinases in nitrogen and carbon metabolism. An extensive backbone of kinase-kinase interactions cross-connects the proteome and may serve to coordinate diverse cellular responses.