TY  - JOUR
A1  - Bazihizina, Nadia
A1  - Böhm, Jennifer
A1  - Messerer, Maxim
A1  - Stigloher, Christian
A1  - Müller, Heike M.
A1  - Cuin, Tracey Ann
A1  - Maierhofer, Tobias
A1  - Cabot, Joan
A1  - Mayer, Klaus F. X.
A1  - Fella, Christian
A1  - Huang, Shouguang
A1  - Al‐Rasheid, Khaled A. S.
A1  - Alquraishi, Saleh
A1  - Breadmore, Michael
A1  - Mancuso, Stefano
A1  - Shabala, Sergey
A1  - Ache, Peter
A1  - Zhang, Heng
A1  - Zhu, Jian‐Kang
A1  - Hedrich, Rainer
A1  - Scherzer, Sönke
T1  - Stalk cell polar ion transport provide for bladder‐based salinity tolerance in Chenopodium quinoa
JF  - New Phytologist
N2  - Chenopodium quinoa uses epidermal bladder cells (EBCs) to sequester excess salt. Each EBC complex consists of a leaf epidermal cell, a stalk cell, and the bladder.

Under salt stress, sodium (Na\(^{+}\)), chloride (Cl\(^{−}\)), potassium (K\(^{+}\)) and various metabolites are shuttled from the leaf lamina to the bladders. Stalk cells operate as both a selectivity filter and a flux controller.

In line with the nature of a transfer cell, advanced transmission electron tomography, electrophysiology, and fluorescent tracer flux studies revealed the stalk cell’s polar organization and bladder‐directed solute flow.

RNA sequencing and cluster analysis revealed the gene expression profiles of the stalk cells. Among the stalk cell enriched genes, ion channels and carriers as well as sugar transporters were most pronounced. Based on their electrophysiological fingerprint and thermodynamic considerations, a model for stalk cell transcellular transport was derived.
KW  - halophyte
KW  - polar ion transport
KW  - quinoa
KW  - salt tolerance
KW  - stalk cell
Y1  - 2022
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-287222
VL  - 235
IS  - 5
SP  - 1822
EP  - 1835
ER  - 
TY  - JOUR
A1  - Liu, Yi
A1  - Maierhofer, Tobias
A1  - Rybak, Katarzyna
A1  - Sklenar, Jan
A1  - Breakspear, Andy
A1  - Johnston, Matthew G.
A1  - Fliegmann, Judith
A1  - Huang, Shouguang
A1  - Roelfsema, M. Rob G.
A1  - Felix, Georg
A1  - Faulkner, Christine
A1  - Menke, Frank L.H.
A1  - Geiger, Dietmar
A1  - Hedrich, Rainer
A1  - Robatzek, Silke
T1  - Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure
JF  - eLife
N2  - In plants, antimicrobial immune responses involve the cellular release of anions and are responsible for the closure of stomatal pores. Detection of microbe-associated molecular patterns (MAMPs) by pattern recognition receptors (PRRs) induces currents mediated via slow-type (S-type) anion channels by a yet not understood mechanism. Here, we show that stomatal closure to fungal chitin is conferred by the major PRRs for chitin recognition, LYK5 and CERK1, the receptor-like cytoplasmic kinase PBL27, and the SLAH3 anion channel. PBL27 has the capacity to phosphorylate SLAH3, of which S127 and S189 are required to activate SLAH3. Full activation of the channel entails CERK1, depending on PBL27. Importantly, both S127 and S189 residues of SLAH3 are required for chitin-induced stomatal closure and anti-fungal immunity at the whole leaf level. Our results demonstrate a short signal transduction module from MAMP recognition to anion channel activation, and independent of ABA-induced SLAH3 activation.
KW  - plants
Y1  - 2019
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-202631
VL  - 8
ER  -