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  Autophagy complements metalloprotease FtsH6 in degrading plastid heat shock protein HSP21 during heat stress recovery

Sedaghatmehr, M., Thirumalaikumar, V. P., Kamranfar, I., Schulz, K., Mueller-Roeber, B., Sampathkumar, A., et al. (2021). Autophagy complements metalloprotease FtsH6 in degrading plastid heat shock protein HSP21 during heat stress recovery. Journal of Experimental Botany. doi:10.1093/jxb/erab304.

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Sedaghatmehr, M.1, Author              
Thirumalaikumar, V. P.1, Author              
Kamranfar, Iman2, Author
Schulz, K.1, Author              
Mueller-Roeber, B.3, Author              
Sampathkumar, A.4, Author              
Balazadeh, S.1, Author              
Affiliations:
1Stress Control Networks, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_2435691              
2External Organizations, ou_persistent22              
3Transcription Factors and Gene Regulatory Networks, Cooperative Research Groups, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753316              
4Plant Cell Biology and Microscopy, Infrastructure Groups and Service Units, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_2253647              

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 Abstract: Moderate and temporary heat stresses (HS) prime plants to tolerate, and survive, a subsequent severe HS. Such acquired thermotolerance can be maintained for several days under normal growth conditions, and create a HS memory. We recently demonstrated that plastid-localized small heat shock protein HSP21 is a key component of HS memory in Arabidopsis thaliana. A sustained high abundance of HSP21 during the HS recovery phase extends HS memory. The level of HSP21 is negatively controlled by plastid-localized metalloprotease FtsH6 during HS recovery. Here, we demonstrate that autophagy, a cellular recycling mechanism, exerts additional control over HSP21 degradation. Genetic and chemical disruption of both, metalloprotease activity and autophagy trigger superior HSP21 accumulation, thereby improving memory. Furthermore, we provide evidence that autophagy cargo receptor ATG8-INTERACTING PROTEIN1 (ATI1) is associated with HS memory. ATI1 bodies colocalize with both autophagosomes and HSP21, and their abundance and transport to the vacuole increase during HS recovery. Together, our results provide new insights into the control module for the regulation of HS memory, in which two distinct protein degradation pathways act in concert to degrade HSP21, thereby enabling cells to recover from the HS effect at the cost of reducing the HS memory.

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Language(s): eng - English
 Dates: 2021-07
 Publication Status: Published in print
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 Identifiers: DOI: 10.1093/jxb/erab304
BibTex Citekey: 10.1093/jxb/erab304
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Title: Journal of Experimental Botany
  Other : J. Exp. Bot
Source Genre: Journal
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Publ. Info: Oxford : Oxford University Press [etc.]
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: - Identifier: ISSN: 0022-0957
CoNE: https://pure.mpg.de/cone/journals/resource/954925413883