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Evolutionary conserved cysteines function as cis-acting regulators of Arabidopsis PIN-FORMED 2 distribution

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Retzer, Katarzyna, Lacek, Jozef, Skokan, Roman, Del Genio, Charo I., Vosolsobě, Stanislav, Laňková, Martina, Malínská, Kateřina, Konstantinova, Nataliia, Zažímalová, Eva, Napier, R. (Richard), Petrášek, Jan and Luschnig, Christian (2017) Evolutionary conserved cysteines function as cis-acting regulators of Arabidopsis PIN-FORMED 2 distribution. International Journal of Molecular Sciences, 18 (11). 2274. doi:10.3390/ijms18112274 ISSN 1422-0067.

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Official URL: http://dx.doi.org/10.3390/ijms18112274

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Abstract

Coordination of plant development requires modulation of growth responses that are under control of the phytohormone auxin. PIN-FORMED plasma membrane proteins, involved in intercellular transport of the growth regulator, are key to the transmission of such auxin signals and subject to multilevel surveillance mechanisms, including reversible post-translational modifications. Apart from well-studied PIN protein modifications, namely phosphorylation and ubiquitylation, no further post-translational modifications have been described so far. Here, we focused on root-specific Arabidopsis PIN2 and explored functional implications of two evolutionary conserved cysteines, by a combination of in silico and molecular approaches. PIN2 sequence alignments and modeling predictions indicated that both cysteines are facing the cytoplasm and therefore would be accessible to redox status-controlled modifications. Notably, mutant pin2C−A alleles retained functionality, demonstrated by their ability to almost completely rescue defects of a pin2 null allele, whereas high resolution analysis of pin2C−A localization revealed increased intracellular accumulation, and altered protein distribution within plasma membrane micro-domains. The observed effects of cysteine replacements on root growth and PIN2 localization are consistent with a model in which redox status-dependent cysteine modifications participate in the regulation of PIN2 mobility, thereby fine-tuning polar auxin transport. View Full-Text

Item Type: Journal Article
Subjects: Q Science > QK Botany
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Auxin -- Molecular aspects, Arabidopsis, Cysteine
Journal or Publication Title: International Journal of Molecular Sciences
Publisher: M D P I AG
ISSN: 1422-0067
Official Date: 29 October 2017
Dates:
DateEvent
29 October 2017Published
26 October 2017Accepted
Volume: 18
Number: 11
Article Number: 2274
DOI: 10.3390/ijms18112274
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 9 November 2017
Date of first compliant Open Access: 9 November 2017
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
P25931Austrian Science Fundhttp://dx.doi.org/10.13039/501100002428
P305/11/0797Czech Science Foundationhttp://dx.doi.org/10.13039/501100001824
LO1417Ministerstvo Školství, Mládeže a Tělovýchovyhttp://dx.doi.org/10.13039/501100001823
CZ.2.16/3.1.00/21519European Commissionhttp://dx.doi.org/10.13039/501100000780
CZ.02.1.01/0.0/0.0/16_013/0001802European Regional Development Fundhttp://dx.doi.org/10.13039/501100008530
PPLZAkademie ved Ceské Republikyhttp://dx.doi.org/10.13039/501100004240
Docfforte fellowshipAkademie ved Ceské Republikyhttp://dx.doi.org/10.13039/501100004240

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