{"doi":"10.1111/nph.18913","title":"<scp>MPK12</scp> in stomatal <scp>CO<sub>2</sub></scp> signaling: function beyond its kinase activity","abstract":"Summary 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 CO 2 concentration. However, whether MPK12 kinase activity is required for regulation of CO 2 ‐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 CO 2 signaling that relies on allosteric inhibition of HT1. We show that CO 2 /HCO 3 − ‐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 CO 2 ‐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 CO 2 /HCO 3 − 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 CO 2 concentration.","journal":"New Phytologist","year":2023,"id":335218,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":20,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9529,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2023-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1064596,"name":"Yuh‐Shuh Wang","orcid":"0000-0002-9193-1235","position":1,"is_corresponding":false},{"id":226499,"name":"Yohei Takahashi","orcid":"0000-0002-9406-4093","position":2,"is_corresponding":false},{"id":1064597,"name":"Katarina Kuusk","orcid":"0000-0001-7240-4555","position":3,"is_corresponding":false},{"id":1064598,"name":"Karnelia Paul","orcid":"0000-0002-3921-7800","position":4,"is_corresponding":false},{"id":1064599,"name":"Triinu Arjus","orcid":"0000-0003-2702-251X","position":5,"is_corresponding":false},{"id":1064600,"name":"Oleksii Yadlos","orcid":"0000-0002-9476-7805","position":6,"is_corresponding":false},{"id":226500,"name":"Julian I. Schroeder","orcid":"0000-0002-3283-5972","position":7,"is_corresponding":false},{"id":1064601,"name":"Ivar Ilves","orcid":"0000-0002-1747-9973","position":8,"is_corresponding":false},{"id":1064602,"name":"Alfonso T. García‐Sosa","orcid":"0000-0003-0542-4446","position":9,"is_corresponding":false},{"id":284844,"name":"Hannes Kollist","orcid":"0000-0002-6895-3583","position":10,"is_corresponding":false},{"id":1064595,"name":"Chung‐Yueh Yeh","orcid":"0000-0003-4771-4222","position":0,"is_corresponding":true}],"reference_count":39,"raw_metadata":null,"created_at":"2026-07-19T01:09:58.338267Z","pmid":"36978283","pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}