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The MAPK substrate MASS proteins regulate stomatal development in Arabidopsis


Autoři: Xueyi Xue aff001;  Chao Bian aff001;  Xiaoyu Guo aff001;  Rong Di aff002;  Juan Dong aff001
Působiště autorů: The Waksman Institute of Microbiology, Rutgers, the State University of New Jersey; Piscataway, New Jersey, United States of America aff001;  Department of Plant Biology, Rutgers, the State University of New Jersey, New Brunswick, New Jersey, United States of America aff002
Vyšlo v časopise: The MAPK substrate MASS proteins regulate stomatal development in Arabidopsis. PLoS Genet 16(4): e32767. doi:10.1371/journal.pgen.1008706
Kategorie: Research Article
doi: https://doi.org/10.1371/journal.pgen.1008706

Souhrn

Stomata are specialized pores in the epidermis of the aerial parts of a plant, where stomatal guard cells close and open to regulate gas exchange with the atmosphere and restrict excessive water vapor from the plant. The production and patterning of the stomatal lineage cells in higher plants are influenced by the activities of the widely-used mitogen-activated protein kinase (MAPK) signaling components. The phenotype caused by the loss-of-function mutations suggested pivotal roles of the canonical MAPK pathway in the suppression of stomatal formation and regulation of stomatal patterning in Arabidopsis, whilst the cell type-specific manipulation of individual MAPK components revealed the existence of a positive impact on stomatal production. Among a large number of putative MAPK substrates in plants, the nuclear transcription factors SPEECHLESS (SPCH) and SCREAM (SCRM) are targets of MAPK 3 and 6 (MPK3/6) in the inhibition of stomatal formation. The polarity protein BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE (BASL) is phosphorylated by MPK3/6 for localization and function in driving divisional asymmetries. Here, by functionally characterizing three MAPK SUBSTRATES IN THE STOMATAL LINEAGE (MASS) proteins, we establish that they are plasma membrane-associated, positive regulators of stomatal production. MPK6 can phosphorylate the MASS proteins in vitro and mutating the putative substrate sites interferes the subcellular partition and function of MASS in planta. Our fine-scale domain analyses identify critical subdomains of MASS2 required for specific subcellular localization and biological function, respectively. Furthermore, our data indicate that the MASS proteins may directly interact with the MAPKK Kinase YODA (YDA) at the plasma membrane. Thus, the deeply conserved MASS proteins are tightly connected with MAPK signaling in Arabidopsis to fine-tune stomatal production and patterning, providing a functional divergence of the YDA-MPK3/6 cascade in the regulation of plant developmental processes.

Klíčová slova:

Arabidopsis thaliana – Cell membranes – Epidermis – MAPK signaling cascades – Membrane proteins – Phosphorylation – Stomata – Plant cotyledon


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