期刊
PLANT AND CELL PHYSIOLOGY
卷 57, 期 11, 页码 2245-2254出版社
OXFORD UNIV PRESS
DOI: 10.1093/pcp/pcw170
关键词
Auxin receptor; Buffering; HSP90; Phenotypic variation; TIR1
资金
- Japan Society for the Promotion of Science (JSPS) [KAKENHI] [19770040, 25440146, 13J10800, 23120520, 25120718, 22000014, 22120007]
- Grants-in-Aid for Scientific Research [19770040, 15H05776, 13J10800] Funding Source: KAKEN
Heat shock protein 90 (HSP90) is a molecular chaperone that is required for the function of various substrate proteins, also known as client proteins. It is proposed that HSP90 buffers or hides phenotypic variations in animals and plants by masking mutations in some of its client proteins. However, none of the client proteins with cryptic mutations has been identified to date. Here, we identify the first client protein example by which HSP90 buffers a mutation: the auxin receptor transport inhibitor response 1 (TIR1). TIR1 interacts with HSP90 in the nucleus. An HSP90-specific inhibitor abolished the nuclear localization of TIR1 and the auxin-induced degradation of a TIR1-substrate, indicating that TIR1 is an HSP90 client protein. Plants with a null mutation in the TIR1 gene had a defect in auxin response, whereas plants with a point mutation in the TIR1 gene responded to auxin treatment in young seedlings, but a cryptic defect in its auxin response was exposed with HSP90 inhibitor treatment. These results demonstrate that HSP90 masks a point mutation in the auxin receptor TIR1 and thereby buffers auxin-responsive phenotypes.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据