The MAPK substrate MASS proteins regulate stomatal development in Arabidopsis.


Journal

PLoS genetics
ISSN: 1553-7404
Titre abrégé: PLoS Genet
Pays: United States
ID NLM: 101239074

Informations de publication

Date de publication:
04 2020
Historique:
received: 26 08 2019
accepted: 04 03 2020
revised: 14 04 2020
pubmed: 3 4 2020
medline: 4 8 2020
entrez: 3 4 2020
Statut: epublish

Résumé

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.

Identifiants

pubmed: 32240168
doi: 10.1371/journal.pgen.1008706
pii: PGENETICS-D-19-01431
pmc: PMC7156110
doi:

Substances chimiques

Arabidopsis Proteins 0
BASL protein, Arabidopsis 0
Basic Helix-Loop-Helix Transcription Factors 0
Cell Cycle Proteins 0
SPEECHLESS protein, Arabidopsis 0
MAP Kinase Kinase Kinases EC 2.7.11.25
YODA protein, Arabidopsis EC 2.7.11.25

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e1008706

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM109080
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM131827
Pays : United States

Déclaration de conflit d'intérêts

The authors have declared that no competing interests exist.

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Auteurs

Xueyi Xue (X)

The Waksman Institute of Microbiology, Rutgers, the State University of New Jersey; Piscataway, New Jersey, United States of America.

Chao Bian (C)

The Waksman Institute of Microbiology, Rutgers, the State University of New Jersey; Piscataway, New Jersey, United States of America.
Department of Plant Biology, Rutgers, the State University of New Jersey, New Brunswick, New Jersey, United States of America.

Xiaoyu Guo (X)

The Waksman Institute of Microbiology, Rutgers, the State University of New Jersey; Piscataway, New Jersey, United States of America.

Rong Di (R)

Department of Plant Biology, Rutgers, the State University of New Jersey, New Brunswick, New Jersey, United States of America.

Juan Dong (J)

The Waksman Institute of Microbiology, Rutgers, the State University of New Jersey; Piscataway, New Jersey, United States of America.
Department of Plant Biology, Rutgers, the State University of New Jersey, New Brunswick, New Jersey, United States of America.

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Classifications MeSH