Journal article
Phosphorylation of the dimeric cytoplasmic domain of the phytosulfokine receptor, PSKR1
V Muleya, C Marondedze, JI Wheeler, L Thomas, YF Mok, MDW Griffin, DT Manallack, L Kwezi, KS Lilley, C Gehring, HR Irving
Biochemical Journal | PORTLAND PRESS LTD | Published : 2016
DOI: 10.1042/BCJ20160593
Abstract
Phytosulfokines (PSKs) are plant peptide hormones that co-regulate plant growth, differentiation and defense responses. PSKs signal through a plasma membrane localized leucine-rich repeat receptor-like kinase (phytosulfokine receptor 1, PSKR1) that also contains a functional cytosolic guanylate cyclase with its cyclase catalytic center embedded within the kinase domain. To functionally characterize this novel type of overlapping dual catalytic function, we investigated the phosphorylation of PSKR1 in vitro. Tandem mass spectrometry of the cytoplasmic domain of PSKR1 (PSKR1cd) revealed at least 11 phosphorylation sites (8 serines, 2 threonines and 1 tyrosine) within the PSKR1cd. Phosphomimeti..
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Awarded by Wellcome Trust
Funding Acknowledgements
Support from the Australian Research Council's Discovery funding scheme [project numbers DP0878194 and DP110104164] and the National Research Foundation South Africa [grant numbers 78843; IRF2009021800047] is gratefully acknowledged. V.M. was supported by a scholarship from the Monash Institute of Pharmaceutical Sciences. M.D.W.G. is the recipient of an Australian Research Council Post-Doctoral Fellowship [DP110103528] and the CR Roper Fellowship. C.G. was supported by King Abdullah University of Science and Technology [KAUST; BAS/1/1013-01-01]. The mass spectrometry was performed using equipment purchased via a Wellcome Trust grant [099135/Z/12/Z].