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Dissection of MAPK signaling specificity through protein engineering in a developmental context

Diego L. Wengier, Gregory R. Lampard, View ORCID ProfileDominique C. Bergmann
doi: https://doi.org/10.1101/115592
Diego L. Wengier
1Howard Hughes Medical Institute
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  • For correspondence: dbergmann@stanford.edu dwengier@dna.uba.ar
Gregory R. Lampard
1Howard Hughes Medical Institute
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Dominique C. Bergmann
1Howard Hughes Medical Institute
2Stanford University, Department of Biology, 371 Serra Mall, Stanford, CA 94305, USA
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  • ORCID record for Dominique C. Bergmann
  • For correspondence: dbergmann@stanford.edu dwengier@dna.uba.ar
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Abstract

Mitogen-activated protein kinases (MAPK) signaling affects many processes, some of which have different outcomes in the same cell. In Arabidopsis, activation of a MAPK cascade consisting of YODA, MKK4/5 and MPK3/6 inhibits early stages of stomatal developmental, but this ability is lost at the latest stage when guard mother cells (GMCs) transition to guard cells (GCs). Rather than downregulating cascade components, stomatal precursors must have a mechanism to prevent late stage inhibition because the same MKKs and MPKs mediate other physiological responses. Here, we artificially activated the MAPK cascade using MKK7, another MKK that can modulate stomatal development, and found that inhibition of stomatal development is still possible in GMCs. This suggests that MKK4/5, but not MKK7, are specifically prevented from inhibiting stomatal development. To identify regions of MKKs responsible for cell-type specific regulation, we used a domain swap approach with MKK7 and a battery of in vitro and in vivo kinase assays. We found that N-terminal regions of MKK5 and MKK7 establish specific signal-to-output connections like they do in other organisms, but they do so in combination with previously undescribed modules in the C-terminus. One of these modules encodes the GMC-specific regulation of MKK5, that when swapped with MKK7’s, allows MKK5 to mediate robust inhibition of late stomatal development. Because MKK structure is conserved across species, the identification of new MKK specificity modules and signaling rules furthers our understanding of how eukaryotes create specificity in complex biological systems.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted March 09, 2017.
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Dissection of MAPK signaling specificity through protein engineering in a developmental context
Diego L. Wengier, Gregory R. Lampard, Dominique C. Bergmann
bioRxiv 115592; doi: https://doi.org/10.1101/115592
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Dissection of MAPK signaling specificity through protein engineering in a developmental context
Diego L. Wengier, Gregory R. Lampard, Dominique C. Bergmann
bioRxiv 115592; doi: https://doi.org/10.1101/115592

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