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Autophosphorylation of gatekeeper tyrosine by symbiosis receptor kinase
Author(s) -
Samaddar Sandip,
Dutta Ayan,
Sinharoy Senjuti,
Paul Anindita,
Bhattacharya Avisek,
Saha Sudip,
Chien Ko-yi,
Goshe Michael B.,
DasGupta Maitrayee
Publication year - 2013
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.2013.07.050
Subject(s) - autophosphorylation , receptor tyrosine kinase , tyrosine kinase , chemistry , microbiology and biotechnology , ror1 , platelet derived growth factor receptor , receptor , biochemistry , kinase , biology , protein kinase a , growth factor
Plant receptor‐like kinases (RLKs) share their evolutionary origin with animal interleukin‐1 receptor‐associated kinase (IRAK)/Pelle family of soluble kinases and are distinguished by having tyrosine as ‘gatekeeper’. This position is adjacent to the hinge region and is hidden in a hydrophobic pocket of the catalytic cleft of protein kinases and is therefore least probable to be a target for any modification. This communication illustrates the accessibility of the gatekeeper site (Y670) towards both autophosphorylation and dephosphorylation in the recombinant cytoplasmic domain of symbiosis receptor kinase from Arachis hypogaea ( Ah SYMRK). Autophosphorylation on gatekeeper tyrosine was detected prior to extraction but never under in vitro conditions. We hypothesize gatekeeper phosphorylation to be associated with synthesis/maturation of Ah SYMRK and this phenomenon may be prevalent among RLKs.