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AtSERPIN1 is an inhibitor of the metacaspase AtMC1-mediated cell death and autocatalytic processing in planta

Saul Lema Asqui, Dominique Vercammen UGent, Irene Serrano, Marc Valls, Susana Rivas, Frank Van Breusegem UGent, Frank L. Conlon, Jeffery L. Dangl and Nuria S. Coll (2018) NEW PHYTOLOGIST. 218(3). p.1156-1166
abstract
The hypersensitive response (HR) is a localized programmed cell death phenomenon that occurs in response to pathogen recognition at the site of attempted invasion. Despite more than a century of research on HR, little is known about how it is so tightly regulated and how it can be contained spatially to a few cells. AtMC1 is an Arabidopsis thaliana plant metacaspase that positively regulates the HR. Here, we used an unbiased approach to identify new AtMC1 regulators. Immunoaffinity purification of AtMC1-containing complexes led us to the identification of the protease inhibitor AtSerpin1. Our data clearly showed that coimmunoprecipitation between AtMC1 and AtSerpin1 and formation of a complex between them was lost upon mutation of the AtMC1 catalytic site, and that the AtMC1 prodomain was not required for the interaction. AtSerpin1 blocked AtMC1 self-processing and inhibited AtMC1-mediated cell death. Our results constitute an invivo example of a Serpin acting as a suicide inhibitor in plants, reminiscent of the activity of animal or viral serpins on immune/cell death regulators, including caspase-1. These results indicate a conserved function of a protease inhibitor on cell death regulators from different kingdoms with unrelated modes of action (i.e. caspases vs metacaspases).
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
GATEWAY BINARY VECTORS, ARABIDOPSIS-THALIANA, CRYSTAL-STRUCTURE, FLUORESCENT PROTEIN, TRYPANOSOMA-BRUCEI, TRANSFORMATION, FAMILIES, DISEASE, GENE, INFLAMMATION, hypersensitive response (HR), metacaspase, plant-pathogen interactions, programmed cell death, protease, serpin
journal title
NEW PHYTOLOGIST
New Phytol.
volume
218
issue
3
pages
11 pages
publisher
Wiley
place of publication
Hoboken
Web of Science type
Article
Web of Science id
000430127000027
ISSN
0028-646X
1469-8137
DOI
10.1111/nph.14446
project
Biotechnology for a sustainable economy (Bio-Economy)
language
English
UGent publication?
yes
classification
U
id
8561873
handle
http://hdl.handle.net/1854/LU-8561873
date created
2018-05-15 11:53:45
date last changed
2018-05-15 11:53:45
@article{8561873,
  abstract     = {The hypersensitive response (HR) is a localized programmed cell death phenomenon that occurs in response to pathogen recognition at the site of attempted invasion. Despite more than a century of research on HR, little is known about how it is so tightly regulated and how it can be contained spatially to a few cells. AtMC1 is an Arabidopsis thaliana plant metacaspase that positively regulates the HR. Here, we used an unbiased approach to identify new AtMC1 regulators. Immunoaffinity purification of AtMC1-containing complexes led us to the identification of the protease inhibitor AtSerpin1. Our data clearly showed that coimmunoprecipitation between AtMC1 and AtSerpin1 and formation of a complex between them was lost upon mutation of the AtMC1 catalytic site, and that the AtMC1 prodomain was not required for the interaction. AtSerpin1 blocked AtMC1 self-processing and inhibited AtMC1-mediated cell death. Our results constitute an invivo example of a Serpin acting as a suicide inhibitor in plants, reminiscent of the activity of animal or viral serpins on immune/cell death regulators, including caspase-1. These results indicate a conserved function of a protease inhibitor on cell death regulators from different kingdoms with unrelated modes of action (i.e. caspases vs metacaspases).},
  author       = {Lema Asqui, Saul and Vercammen, Dominique and Serrano, Irene and Valls, Marc and Rivas, Susana and Van Breusegem, Frank and Conlon, Frank L. and Dangl, Jeffery L. and Coll, Nuria S.},
  issn         = {0028-646X},
  journal      = {NEW PHYTOLOGIST},
  keyword      = {GATEWAY BINARY VECTORS,ARABIDOPSIS-THALIANA,CRYSTAL-STRUCTURE,FLUORESCENT PROTEIN,TRYPANOSOMA-BRUCEI,TRANSFORMATION,FAMILIES,DISEASE,GENE,INFLAMMATION,hypersensitive response (HR),metacaspase,plant-pathogen interactions,programmed cell death,protease,serpin},
  language     = {eng},
  number       = {3},
  pages        = {1156--1166},
  publisher    = {Wiley},
  title        = {AtSERPIN1 is an inhibitor of the metacaspase AtMC1-mediated cell death and autocatalytic processing in planta},
  url          = {http://dx.doi.org/10.1111/nph.14446},
  volume       = {218},
  year         = {2018},
}

Chicago
Lema Asqui, Saul, Dominique Vercammen, Irene Serrano, Marc Valls, Susana Rivas, Frank Van Breusegem, Frank L. Conlon, Jeffery L. Dangl, and Nuria S. Coll. 2018. “AtSERPIN1 Is an Inhibitor of the Metacaspase AtMC1-mediated Cell Death and Autocatalytic Processing in Planta.” New Phytologist 218 (3): 1156–1166.
APA
Lema Asqui, S., Vercammen, D., Serrano, I., Valls, M., Rivas, S., Van Breusegem, F., Conlon, F. L., et al. (2018). AtSERPIN1 is an inhibitor of the metacaspase AtMC1-mediated cell death and autocatalytic processing in planta. NEW PHYTOLOGIST, 218(3), 1156–1166.
Vancouver
1.
Lema Asqui S, Vercammen D, Serrano I, Valls M, Rivas S, Van Breusegem F, et al. AtSERPIN1 is an inhibitor of the metacaspase AtMC1-mediated cell death and autocatalytic processing in planta. NEW PHYTOLOGIST. Hoboken: Wiley; 2018;218(3):1156–66.
MLA
Lema Asqui, Saul, Dominique Vercammen, Irene Serrano, et al. “AtSERPIN1 Is an Inhibitor of the Metacaspase AtMC1-mediated Cell Death and Autocatalytic Processing in Planta.” NEW PHYTOLOGIST 218.3 (2018): 1156–1166. Print.