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FEBS Lett. 2013 Sep 17;587(18):2972-9. doi: 10.1016/j.febslet.2013.07.050. Epub 2013 Aug 17.

Autophosphorylation of gatekeeper tyrosine by symbiosis receptor kinase.

Author information

1
Department of Biochemistry, University of Calcutta, Kolkata, India.

Abstract

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 (AhSYMRK). 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 AhSYMRK and this phenomenon may be prevalent among RLKs.

KEYWORDS:

Autophosphorylation; CD; CIAP; Gatekeeper residue; IRAK; KD; RLK; Receptor-like kinase; SYMRK; Symbiosis receptor kinase; TKL; Trx; Tyrosine kinase-like; calf intestinal alkaline phosphatase; cytoplasmic domain; interleukin-1 receptor-associated kinase; kinase domain; receptor-like kinase; symbiosis receptor kinase; thioredoxin; tyrosine-kinase like

PMID:
23962520
DOI:
10.1016/j.febslet.2013.07.050
[Indexed for MEDLINE]
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