Coevolving MAPK and PID phosphosites indicate an ancient environmental control of PIN auxin transporters in land plants

Plant growth flexibly adapts to environmental conditions, implying cross‐talk between environmental signalling and developmental regulation. Here, we show that the PIN auxin efflux carrier family possesses three highly conserved putative mitogen‐activated protein kinase (MAPK) sites adjacent to the...

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Bibliographic Details
Published in:FEBS letters 2018-01, Vol.592 (1), p.89-102
Main Authors: Dory, Magdalena, Hatzimasoura, Elizabeth, Kállai, Brigitta M., Nagy, Szilvia K., Jäger, Katalin, Darula, Zsuzsanna, Nádai, Tímea V., Mészáros, Tamás, López‐Juez, Enrique, Barnabás, Beáta, Palme, Klaus, Bögre, László, Ditengou, Franck A., Dóczi, Róbert
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Arabidopsis
Arabidopsis - genetics
Arabidopsis - metabolism
Binding Sites - genetics
Conserved Sequence
Evolution, Molecular
Indoleacetic Acids - metabolism
MAP kinase
Membrane Transport Proteins - genetics
Membrane Transport Proteins - metabolism
Mitogen-Activated Protein Kinases - genetics
Mitogen-Activated Protein Kinases - metabolism
Phosphorylation
PIN
Plant Development
Plant Proteins - genetics
Plant Proteins - metabolism
Plant Roots - metabolism
Plants - genetics
Plants - metabolism
Plants, Genetically Modified
protein phosphorylation
Protein Serine-Threonine Kinases - genetics
Protein Serine-Threonine Kinases - metabolism
Protoplasts - metabolism
Research Letter
Research Letters
signalling
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Summary:Plant growth flexibly adapts to environmental conditions, implying cross‐talk between environmental signalling and developmental regulation. Here, we show that the PIN auxin efflux carrier family possesses three highly conserved putative mitogen‐activated protein kinase (MAPK) sites adjacent to the phosphorylation sites of the well‐characterised AGC kinase PINOID, which regulates the polar localisation of PINs and directional auxin transport, thereby underpinning organ growth. The conserved sites of PIN1 are phosphorylated in vitro by two environmentally activated MAPKs, MPK4 and MPK6. In contrast to AGC kinases, MAPK‐mediated phosphorylation of PIN1 at adjacent sites leads to a partial loss of the plasma membrane localisation of PIN1. MAPK‐mediated modulation of PIN trafficking may participate in environmental adjustment of plant growth.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12929