MPK12 in stomatal CO2 signaling function beyond its kinase activity

MPK12 in stomatal CO2 signaling : function beyond its kinase activity

© 2023 The Authors. New Phytologist © 2023 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 239(2023), 1 vom: 01. Juli, Seite 146-158
1. Verfasser: Yeh, Chung-Yueh (VerfasserIn)
Weitere Verfasser: Wang, Yuh-Shuh, Takahashi, Yohei, Kuusk, Katarina, Paul, Karnelia, Arjus, Triinu, Yadlos, Oleksii, Schroeder, Julian I, Ilves, Ivar, Garcia-Sosa, Alfonso T, Kollist, Hannes
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2023
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, N.I.H., Extramural CO2 signaling HT1 MAP kinase 12 allosteric inhibition guard cell noncatalytic activity mehr... stomata Arabidopsis Proteins Mitogen-Activated Protein Kinases EC 2.7.11.24 Carbon Dioxide 142M471B3J
Beschreibung
Zusammenfassung:© 2023 The Authors. New Phytologist © 2023 New Phytologist Foundation.
Protein phosphorylation is a major molecular switch involved in the regulation of stomatal opening and closure. Previous research defined interaction between MAP kinase 12 and Raf-like kinase HT1 as a required step for stomatal movements caused by changes in CO2 concentration. However, whether MPK12 kinase activity is required for regulation of CO2 -induced stomatal responses warrants in-depth investigation. We apply genetic, biochemical, and structural modeling approaches to examining the noncatalytic role of MPK12 in guard cell CO2 signaling that relies on allosteric inhibition of HT1. We show that CO2 /HCO3 - -enhanced MPK12 interaction with HT1 is independent of its kinase activity. By analyzing gas exchange of plant lines expressing various kinase-dead and constitutively active versions of MPK12 in a plant line where MPK12 is deleted, we confirmed that CO2 -dependent stomatal responses rely on MPK12's ability to bind to HT1, but not its kinase activity. We also demonstrate that purified MPK12 and HT1 proteins form a heterodimer in the presence of CO2 /HCO3 - and present structural modeling that explains the MPK12:HT1 interaction interface. These data add to the model that MPK12 kinase-activity-independent interaction with HT1 functions as a molecular switch by which guard cells sense changes in atmospheric CO2 concentration
Beschreibung:Date Completed 02.06.2023
Date Revised 02.07.2024
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.18913