| Literature DB >> 34297043 |
Henning Mühlenbeck1, Kyle W Bender1,2, Cyril Zipfel1,2.
Abstract
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.Entities:
Keywords: phosphorylation/dephosphorylation; receptor tyrosine kinases; receptors
Year: 2021 PMID: 34297043 DOI: 10.1042/BCJ20210202
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857