Phytosulfokine-α Controls Hypocotyl Length and Cell Expansion in Arabidopsis thaliana through Phytosulfokine Receptor 1

The disulfated peptide growth factor phytosulfokine-alpha (PSK-alpha) is perceived by LRR receptor kinases. In this study, a role for PSK signaling through PSK receptor PSKR1 in Arabidopsis thaliana hypocotyl cell elongation is established. Hypocotyls of etiolated pskr1-2 and pskr1-3 seedlings, but not of pskr2-1 seedlings were shorter than wt due to reduced cell elongation. Treatment with PSK-alpha did not promote hypocotyl growth indicating that PSK levels were saturating. Tyrosylprotein sulfotransferase (TPST) is responsible for sulfation and hence activation of the PSK precursor. The tpst-1 mutant displayed shorter hypocotyls with shorter cells than wt. Treatment of tpst-1 seedlings with PSK-alpha partially restored elongation growth in a dose-dependent manner. Hypocotyl elongation was significantly enhanced in tpst-1 seedlings at nanomolar PSK-alpha concentrations. Cell expansion was studied in hypocotyl protoplasts. WT and pskr2-1 protoplasts expanded in the presence of PSK-alpha in a dose-dependent manner. By contrast, pskr1-2 and pskr1-3 protoplasts were unresponsive to PSK-alpha. Protoplast swelling in response to PSK-alpha was unaffected by ortho-vanadate, which inhibits the plasma membrane H+-ATPase. In maize (Zea mays L.), coleoptile protoplast expansion was similarly induced by PSK-alpha in a dose-dependent manner and was dependent on the presence of K+ in the media. In conclusion, PSK-alpha signaling of hypocotyl elongation and protoplast expansion occurs through PSKR1 and likely involves K+ uptake, but does not require extracellular acidification by the plasma membrane H+-ATPase.