CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASES: their evolution, structure, and roles in stress response and development

Author:

Zeiner Adam12ORCID,Colina Francisco J1ORCID,Citterico Matteo3ORCID,Wrzaczek Michael13ORCID

Affiliation:

1. Institute of Plant Molecular Biology, Biology Centre, Czech Academy of Sciences , 370 05 České Budějovice , Czech Republic

2. Faculty of Science, University of South Bohemia , 370 05 České Budějovice , Czech Republic

3. Organismal and Evolutionary Biology Research Programme, Faculty of Biological and Environmental Sciences, and Viikki Plant Science Center, University of Helsinki , FI-00014 Helsinki , Finland

Abstract

Abstract Plant-specific receptor-like protein kinases (RLKs) are central components for sensing the extracellular microenvironment. CYSTEINE-RICH RLKs (CRKs) are members of one of the biggest RLK subgroups. Their physiological and molecular roles have only begun to be elucidated, but recent studies highlight the diverse types of proteins interacting with CRKs, as well as the localization of CRKs and their lateral organization within the plasma membrane. Originally the DOMAIN OF UNKNOWN FUNCTION 26 (DUF26)-containing extracellular region of the CRKs was proposed to act as a redox sensor, but the potential activating post-translational modification or ligands perceived remain elusive. Here, we summarize recent progress in the analysis of CRK evolution, molecular function, and role in plant development, abiotic stress responses, plant immunity, and symbiosis. The currently available information on CRKs and related proteins suggests that the CRKs are central regulators of plant signaling pathways. However, more research using classical methods and interdisciplinary approaches in various plant model species, as well as structural analyses, will not only enhance our understanding of the molecular function of CRKs, but also elucidate the contribution of other cellular components in CRK-mediated signaling pathways.

Funder

University of Helsinki, Academy of Finland

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Physiology

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