The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization

Steffens A, Bräutigam A, Jakoby M, Hülskamp M (2015)
PLOS Biology 13(7): e1002188.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
OA 14.16 MB
Autor/in
; ; ;
Abstract / Bemerkung
Members of the highly conserved class of BEACH domain containing proteins (BDCPs) have been established as broad facilitators of protein-protein interactions and membrane dynamics in the context of human diseases like albinism, bleeding diathesis, impaired cellular immunity, cancer predisposition, and neurological dysfunctions. Also, the Arabidopsis thaliana BDCP SPIRRIG (SPI) is important for membrane integrity, as spi mutants exhibit split vacuoles. In this work, we report a novel molecular function of the BDCP SPI in ribonucleoprotein particle formation. We show that SPI interacts with the P-body core component DECAPPING PROTEIN 1 (DCP1), associates to mRNA processing bodies (P-bodies), and regulates their assembly upon salt stress. The finding that spi mutants exhibit salt hypersensitivity suggests that the local function of SPI at P-bodies is of biological relevance. Transcriptome-wide analysis revealed qualitative differences in the salt stress-regulated transcriptional response of Col-0 and spi. We show that SPI regulates the salt stress-dependent post-transcriptional stabilization, cytoplasmic agglomeration, and localization to P-bodies of a subset of salt stress-regulated mRNAs. Finally, we show that the PH-BEACH domains of SPI and its human homolog FAN (Factor Associated with Neutral sphingomyelinase activation) interact with DCP1 isoforms from plants, mammals, and yeast, suggesting the evolutionary conservation of an association of BDCPs and P-bodies.
Erscheinungsjahr
2015
Zeitschriftentitel
PLOS Biology
Band
13
Ausgabe
7
Art.-Nr.
e1002188
ISSN
1545-7885
Page URI
https://pub.uni-bielefeld.de/record/2915133

Zitieren

Steffens A, Bräutigam A, Jakoby M, Hülskamp M. The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization. PLOS Biology. 2015;13(7): e1002188.
Steffens, A., Bräutigam, A., Jakoby, M., & Hülskamp, M. (2015). The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization. PLOS Biology, 13(7), e1002188. doi:10.1371/journal.pbio.1002188
Steffens, A., Bräutigam, A., Jakoby, M., and Hülskamp, M. (2015). The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization. PLOS Biology 13:e1002188.
Steffens, A., et al., 2015. The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization. PLOS Biology, 13(7): e1002188.
A. Steffens, et al., “The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization”, PLOS Biology, vol. 13, 2015, : e1002188.
Steffens, A., Bräutigam, A., Jakoby, M., Hülskamp, M.: The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization. PLOS Biology. 13, : e1002188 (2015).
Steffens, Alexandra, Bräutigam, Andrea, Jakoby, Marc, and Hülskamp, Martin. “The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and Localization”. PLOS Biology 13.7 (2015): e1002188.
Alle Dateien verfügbar unter der/den folgenden Lizenz(en):
Creative Commons Namensnennung 4.0 International Public License (CC-BY 4.0):
Volltext(e)
Access Level
OA Open Access
Zuletzt Hochgeladen
2019-09-06T09:18:54Z
MD5 Prüfsumme
d5f3bcf3dccaeeeb8bf212dec4ecbde6

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 26133670
PubMed | Europe PMC

Suchen in

Google Scholar