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The PINOID protein kinase regulates organ development in Arabidopsis by enhancing polar auxin transport

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Benjamins, René, Quint, Ab, Weijers, Dolf, Hooykaas, Paul, Offringa, Remko·2001·Development
DOI 10.1242/dev.128.20.4057
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Abstract

Arabidopsis pinoid mutants show a strong phenotypic resemblance to the pin-formed mutant that is disrupted in polar auxin transport. The PINOID gene was recently cloned and found to encode a protein-serine/threonine kinase. Here we show that the PINOID gene is inducible by auxin and that the protein kinase is present in the primordia of cotyledons, leaves and floral organs and in vascular tissue in developing organs or proximal to meristems. Overexpression of PINOID under the control of the constitutive CaMV 35S promoter (35S::PID) resulted in phenotypes also observed in mutants with altered sensitivity to or transport of auxin. A remarkable characteristic of high expressing 35S::PID seedlings was a frequent collapse of the primary root meristem. This event triggered lateral root formation, a process that was initially inhibited in these seedlings. Both meristem organisation and growth of the primary root were rescued when seedlings were grown in the presence of polar auxin transport inhibitors, such as naphthylphtalamic acid (NPA). Moreover, ectopic expression of PINOID cDNA under control of the epidermis-specific LTP1 promoter provided further evidence for the NPA-sensitive action of PINOID. The results presented here indicate that PINOID functions as a positive regulator of polar auxin transport. We propose that PINOID is involved in the fine-tuning of polar auxin transport during organ formation in response to local auxin concentrations.

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Cited by

Metadata

Authors
Benjamins, R., Quint, A., Weijers, D., Hooykaas, P., & Offringa, R.
Venue
Development
Publisher
The Company of Biologists
Published
2001-10-15
Volume
128
Issue
20
Pages
4057-4067
ISSN
  • 0950-1991 (ISSN-L)
  • 1477-9129
DOI
10.1242/dev.128.20.4057
OpenAlex
W2165962198
Cited by
457
References
0
FWCI
20.75
Type
journal article
Language
en
Open access
green

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