Overexpression of a stress response membrane protein gene OsSMP1 enhances rice tolerance to salt, cold and heavy metal stress

2021 ◽  
Vol 182 ◽  
pp. 104327
Author(s):  
Shiwei Zheng ◽  
Shengbin Liu ◽  
Jinhua Feng ◽  
Wei Wang ◽  
Yuwei Wang ◽  
...  
PROTEOMICS ◽  
2007 ◽  
Vol 7 (8) ◽  
pp. 1249-1260 ◽  
Author(s):  
Servet Özcan ◽  
Volkan Yıldırım ◽  
Levent Kaya ◽  
Dirk Albrecht ◽  
Dörte Becher ◽  
...  

2021 ◽  
Vol 5 (Supplement_1) ◽  
pp. 687-687
Author(s):  
Emily Turner ◽  
Amanda Furtmann ◽  
Hope Dang ◽  
Destiny DeNicola ◽  
George Sutphin

Abstract Cellular stress is an ever-present aspect of aging and a primary driver of many common age-associated diseases such as cancer, diabetes, or neurodegenerative diseases. As we age, stress-induced damage accumulates over time, along with reduced efficacy of stress response pathways at combatting such damage. Molecular stress response pathways are well studied in the context of individual stressors, but there is a lack of understanding of how these responses change when multiple stressors are encountered at the same time. The goal of our work is to explore the impact of multiple simultaneous stressors on health and survival, and to investigate the underlying molecular pathways involved. To accomplish this, we utilize the nematode Caenorhabditis elegans to monitor lifespan changes in response to various stressors. We simultaneously exposed C. elegans to high concentrations of sodium chloride and cadmium chloride, known to induce osmotic and heavy metal stress, respectively. We found that lifespan is drastically decreased by the combined stress, significantly more so than the reduction in lifespan caused by either individual stress. Our results show that glycerol levels, which are normally increased in response to osmotic stress, are significantly lowered when the two stresses are combined compared to levels detected for osmotic stress alone. This suggests that the presence of cadmium may sensitize worms to sodium and other osmotic stressors by blunting cells’ ability to mount an appropriate molecular response. In ongoing work, we will continue to dissect the mechanisms through which cadmium influences glycerol production and other aspects of osmotic stress response.


2004 ◽  
Vol 2004 (Spring) ◽  
Author(s):  
Walter Schaffner ◽  
Dieter Egli ◽  
Balamurugan Kuppusamy ◽  
Hasmik Yepiskoposyan ◽  
Anan Selvaraj ◽  
...  

2020 ◽  
Vol 117 (35) ◽  
pp. 21319-21327 ◽  
Author(s):  
Linda Lauinger ◽  
Karin Flick ◽  
James L. Yen ◽  
Radhika Mathur ◽  
Peter Kaiser

Organisms can adapt to a broad spectrum of sudden and dramatic changes in their environment. These abrupt changes are often perceived as stress and trigger responses that facilitate survival and eventual adaptation. The ubiquitin–proteasome system (UPS) is involved in most cellular processes. Unsurprisingly, components of the UPS also play crucial roles during various stress response programs. The budding yeast SCFMet30complex is an essential cullin-RING ubiquitin ligase that connects metabolic and heavy metal stress to cell cycle regulation. Cadmium exposure results in the active dissociation of the F-box protein Met30 from the core ligase, leading to SCFMet30inactivation. Consequently, SCFMet30substrate ubiquitylation is blocked and triggers a downstream cascade to activate a specific transcriptional stress response program. Signal-induced dissociation is initiated by autoubiquitylation of Met30 and serves as a recruitment signal for the AAA-ATPase Cdc48/p97, which actively disassembles the complex. Here we show that the UBX cofactor Shp1/p47 is an additional key element for SCFMet30disassembly during heavy metal stress. Although the cofactor can directly interact with the ATPase, Cdc48 and Shp1 are recruited independently to SCFMet30during cadmium stress. An intact UBX domain is crucial for effective SCFMet30disassembly, and a concentration threshold of Shp1 recruited to SCFMet30needs to be exceeded to initiate Met30 dissociation. The latter is likely related to Shp1-mediated control of Cdc48 ATPase activity. This study identifies Shp1 as the crucial Cdc48 cofactor for signal-induced selective disassembly of a multisubunit protein complex to modulate activity.


2013 ◽  
Vol 21 (3) ◽  
pp. 1723-1737 ◽  
Author(s):  
Angela Cicatelli ◽  
Valeria Todeschini ◽  
Guido Lingua ◽  
Stefania Biondi ◽  
Patrizia Torrigiani ◽  
...  

2016 ◽  
Vol 35 (12) ◽  
pp. 776-786 ◽  
Author(s):  
Chengjian Huang ◽  
Jinghua Zhou ◽  
Yucheng Jie ◽  
Hucheng Xing ◽  
Yingli Zhong ◽  
...  

2012 ◽  
Vol 38 (12) ◽  
pp. 1106-1110 ◽  
Author(s):  
Yan-Fei DING ◽  
Cheng ZHU ◽  
Shan-Shan WANG ◽  
Hai-Li LIU

2019 ◽  
Author(s):  
Linda Lauinger ◽  
Karin Flick ◽  
James L. Yen ◽  
Radhika Mathur ◽  
Peter Kaiser

AbstractOrganisms can adapt to a broad spectrum of sudden and dramatic changes in their environment. These abrupt changes are often perceived as stress and trigger responses that facilitate survival and eventual adaptation. The ubiquitin proteasome system (UPS) is involved in most cellular processes. Unsurprisingly, components of the UPS also play crucial roles during various stress response programs. The budding yeast SCFMet30 complex is an essential Cullin-RING ubiquitin ligase that connects metabolic and heavy metal stress to cell cycle regulation. Cadmium exposure results in the active dissociation of the F-box protein Met30 from the core ligase leading to SCFMet30 inactivation. Consequently, SCFMet30 substrate ubiquitylation is blocked and triggers a downstream cascade to activate a specific transcriptional stress response program. Signal-induced dissociation is initiated by autoubiquitylation of Met30 and serves as a recruitment signal for the AAA-ATPase Cdc48/p97, which actively disassembles the complex. Here we show that the UBX cofactor Shp1/p47 is an additional key element for SCFMet30 disassembly during heavy metal stress. Although the cofactor can directly interact with the ATPase, Cdc48 and Shp1 are recruited independently to SCFMet30 during cadmium stress. An intact UBX domain is crucial for effective SCFMet30 disassembly, and a concentration threshold of Shp1 recruited to SCFMet30 needs to be exceeded to initiate Met30 dissociation. The latter is likely related to Shp1-mediated control of Cdc48 ATPase activity. This study identifies Shp1 as the crucial Cdc48 cofactor for signal-induced, selective disassembly of a multi-subunit protein complex to modulate activity.Significance StatementUbiquitylation affects many important cellular processes, and has been linked to a number of human diseases. It has become a synonym for protein degradation, but ubiquitylation also has important non-proteolytic signaling functions. Understanding the molecular concepts that govern ubiquitin signaling is of great importance for development of diagnostics and therapeutics. The cadmium-induced inactivation of the SCFMet30 ubiquitin ligase via the disassembly of the multi-subunit ligase complex, illustrates an example for non-proteolytic signaling pathways. Dissociation is triggered by autoubiquitylation of the F-box protein Met30, which is the recruiting signal for the highly conserved AAA-ATPase Cdc48/p97. Here we show that the UBX cofactor Shp1/p47 is important for this ubiquitin-dependent, active remodeling of a multi-protein complex in response to a specific environmental signal.


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