Identification of Open Stomata1-Interacting Proteins Reveals Interactions with Sucrose Non-fermenting1-Related Protein Kinases2 and with Type 2A Protein Phosphatases That Function in Abscisic Acid Responses
- Univ. of Heidelberg (Germany). Centre for Organismal Studies; Univ. of California, San Diego, CA (United States)
- Univ. of California, San Diego, CA (United States); Scripps Research Inst., La Jolla, CA (United States). Dept. of Chemical Physiology
- Okayama Univ. (Japan); Univ. of California, San Diego, CA (United States)
- Brown Univ., Providence, RI (United States). Dept. of Molecular Biology Cell Biology and Biochemistry
- Scripps Research Inst., La Jolla, CA (United States). Dept. of Chemical Physiology; Univ. of California, San Diego, CA (United States)
- Okayama Univ. (Japan)
- Donald Danforth Plant Science Center, St. Louis, MS (United States). Dept. of Biology
- Univ. of Southern California, Los Angeles, CA (United States)
- Brown Univ., Providence, RI (United States). Dept. of Molecular Biology Cell Biology and Biochemistry; Univ. of California, San Diego, CA (United States)
- Univ. of Heidelberg (Germany). Centre for Organismal Studies
- Scripps Research Inst., La Jolla, CA (United States). Dept. of Chemical Physiology
- Univ. of Southern California, Los Angeles, CA (United States); Univ. of California, San Diego, CA (United States)
The plant hormone abscisic acid (ABA) controls growth and development and regulates plant water status through an established signaling pathway. In the presence of ABA, pyrabactin resistance/regulatory component of ABA receptor proteins inhibit type 2C protein phosphatases (PP2Cs). This, in turn, enables the activation of Sucrose Nonfermenting1-Related Protein Kinases2 (SnRK2). Open Stomata1 (OST1)/SnRK2.6/SRK2E is a major SnRK2-type protein kinase responsible for mediating ABA responses. Arabidopsis (Arabidopsis thaliana) expressing an epitope-tagged OST1 in the recessive ost1-3 mutant background was used for the copurification and identification of OST1-interacting proteins after osmotic stress and ABA treatments. Furthemore, these analyses, which were confirmed using bimolecular fluorescence complementation and coimmunoprecipitation, unexpectedly revealed homo- and heteromerization of OST1 with SnRK2.2, SnRK2.3, OST1, and SnRK2.8. Furthermore, several OST1-complexed proteins were identified as type 2A protein phosphatase (PP2A) subunits and as proteins involved in lipid and galactolipid metabolism. More detailed analyses suggested an interaction network between ABA-activated SnRK2-type protein kinases and several PP2A-type protein phosphatase regulatory subunits. pp2a double mutants exhibited a reduced sensitivity to ABA during seed germination and stomatal closure and an enhanced ABA sensitivity in root growth regulation. Our analyses add PP2A-type protein phosphatases as another class of protein phosphatases to the interaction network of SnRK2-type protein kinases.
- Research Organization:
- Univ. of California, San Diego, CA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- FG02-03ER15449
- OSTI ID:
- 1411727
- Journal Information:
- Plant Physiology (Bethesda), Vol. 169, Issue 1; ISSN 0032-0889
- Publisher:
- American Society of Plant BiologistsCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
Similar Records
ABA Receptors: Past, Present and Future
Molecular identification of BrHAB2a, one of the two AtHAB2-like proteins in Brassica rapa, is an important component of ABA signaling