Calcineurin B-like 3 calcium sensor associates with and inhibits 5 '-methylthioadenosine nucleosidase 2 in Arabidopsis
- Authors
- Ok, Sung Han; Cho, Joo Hyuk; Oh, Seung-Ick; Choi, Mi Na; Ma, Jae-Yeon; Shin, Jeong-Sheop; Kim, Kyung-Nam
- Issue Date
- Sep-2015
- Publisher
- ELSEVIER IRELAND LTD
- Keywords
- Calcium signaling; CBL; CIPK; MTAN; Arabidopsis
- Citation
- PLANT SCIENCE, v.238, pp.228 - 240
- Indexed
- SCIE
SCOPUS
- Journal Title
- PLANT SCIENCE
- Volume
- 238
- Start Page
- 228
- End Page
- 240
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/92693
- DOI
- 10.1016/j.plantsci.2015.06.016
- ISSN
- 0168-9452
- Abstract
- Calcineurin B-like (CBL) proteins constitute a unique family of calcium sensor relays in plants. It is well known that CBLs detect the calcium signals elicited by a variety of abiotic stresses and relay the information to a group of serine/threonine protein kinases called CBL-interacting protein kinases (CIPKs). In this study, we found that a few CBL members can also target another group of enzymes 5'-methylthioadenosine nucleosidases (MTANs), which are encoded by two genes in Arabidopsis, AtMTAN1 and AtMTAN2. In the yeast two-hybrid system, AtMTAN1 interacted with multiple CBL members such as CBL2, CBL3 and CBL6, whereas AtMTAN2 associated exclusively with CBL3. We further demonstrated that the CBL3-AtMTAN2 association occurs in a calcium-dependent manner, which results in a significant decrease in the enzyme activity of the AtMTAN2 protein. Taken together, these results clearly indicate that the CBL family can target at least two distinct groups of enzymes (CIPKs and MTANs), conferring an additional level of complexity on the CBL-mediated signaling networks. In addition, our finding also provides a novel molecular mechanism by which calcium signals are transduced to alter metabolite profiles in plants. (C) 2015 Elsevier Ireland Ltd. All rights reserved.
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