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Gatekeeper tyrosine phosphorylation is autoinhibitory for Symbiosis Receptor Kinase
Author(s) -
Paul Anindita,
Samaddar Sandip,
Bhattacharya Avisek,
Banerjee Anindyajit,
Das Abhishek,
Chakrabarti Saikat,
DasGupta Maitrayee
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.06.056
Subject(s) - autophosphorylation , phosphorylation , receptor tyrosine kinase , tyrosine kinase , tyrosine , chemistry , biochemistry , tyrosine phosphorylation , kinase , microbiology and biotechnology , biology , receptor , protein kinase a
Plant receptor‐like kinases (RLKs) are distinguished by having a tyrosine in the ‘gatekeeper’ position. Previously we reported Symbiosis Receptor Kinase from Arachis hypogaea ( Ah SYMRK) to autophosphorylate on the gatekeeper tyrosine (Y670), though this phosphorylation was not necessary for the kinase activity. Here we report that recombinant catalytic domain of Ah SYMRK with a phosphomimic substitution in the gatekeeper position (Y670E) is catalytically almost inactive and is conformationally quite distinct from the corresponding native enzyme. Additionally, we show that gatekeeper‐phosphorylated Ah SYMRK polypeptides are inactive and depletion of this inactive form leads to activation of intramolecular autophosphorylation of Ah SYMRK. Together, our results suggest gatekeeper tyrosine autophosphorylation to be autoinhibitory for Ah SYMRK.