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Importance of tyrosine phosphorylation for transmembrane signaling in plants

Reversible protein phosphorylation is a widespread post-translational modification fundamental for signaling across all domains of life. Tyrosine (Tyr) phosphorylation has recently emerged as being important for plant receptor kinase (RK)-mediated signaling, particularly during plant immunity. How T...

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Detalles Bibliográficos
Autores principales: Mühlenbeck, Henning, Bender, Kyle W., Zipfel, Cyril
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8331091/
https://www.ncbi.nlm.nih.gov/pubmed/34297043
http://dx.doi.org/10.1042/BCJ20210202
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author Mühlenbeck, Henning
Bender, Kyle W.
Zipfel, Cyril
author_facet Mühlenbeck, Henning
Bender, Kyle W.
Zipfel, Cyril
author_sort Mühlenbeck, Henning
collection PubMed
description Reversible protein phosphorylation is a widespread post-translational modification fundamental for signaling across all domains of life. Tyrosine (Tyr) phosphorylation has recently emerged as being important for plant receptor kinase (RK)-mediated signaling, particularly during plant immunity. How Tyr phosphorylation regulates RK function is however largely unknown. Notably, the expansion of protein Tyr phosphatase and SH2 domain-containing protein families, which are the core of regulatory phospho-Tyr (pTyr) networks in choanozoans, did not occur in plants. Here, we summarize the current understanding of plant RK Tyr phosphorylation focusing on the critical role of a pTyr site (‘VIa-Tyr’) conserved in several plant RKs. Furthermore, we discuss the possibility of metazoan-like pTyr signaling modules in plants based on atypical components with convergent biochemical functions.
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spelling pubmed-83310912021-08-11 Importance of tyrosine phosphorylation for transmembrane signaling in plants Mühlenbeck, Henning Bender, Kyle W. Zipfel, Cyril Biochem J Signaling Reversible protein phosphorylation is a widespread post-translational modification fundamental for signaling across all domains of life. Tyrosine (Tyr) phosphorylation has recently emerged as being important for plant receptor kinase (RK)-mediated signaling, particularly during plant immunity. How Tyr phosphorylation regulates RK function is however largely unknown. Notably, the expansion of protein Tyr phosphatase and SH2 domain-containing protein families, which are the core of regulatory phospho-Tyr (pTyr) networks in choanozoans, did not occur in plants. Here, we summarize the current understanding of plant RK Tyr phosphorylation focusing on the critical role of a pTyr site (‘VIa-Tyr’) conserved in several plant RKs. Furthermore, we discuss the possibility of metazoan-like pTyr signaling modules in plants based on atypical components with convergent biochemical functions. Portland Press Ltd. 2021-07-30 2021-07-23 /pmc/articles/PMC8331091/ /pubmed/34297043 http://dx.doi.org/10.1042/BCJ20210202 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) .
spellingShingle Signaling
Mühlenbeck, Henning
Bender, Kyle W.
Zipfel, Cyril
Importance of tyrosine phosphorylation for transmembrane signaling in plants
title Importance of tyrosine phosphorylation for transmembrane signaling in plants
title_full Importance of tyrosine phosphorylation for transmembrane signaling in plants
title_fullStr Importance of tyrosine phosphorylation for transmembrane signaling in plants
title_full_unstemmed Importance of tyrosine phosphorylation for transmembrane signaling in plants
title_short Importance of tyrosine phosphorylation for transmembrane signaling in plants
title_sort importance of tyrosine phosphorylation for transmembrane signaling in plants
topic Signaling
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8331091/
https://www.ncbi.nlm.nih.gov/pubmed/34297043
http://dx.doi.org/10.1042/BCJ20210202
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