Behead and live long or the tale of cathepsin L

Streubel, Maria Karolin; Bischof, Johannes; Weiss, Richard; Duschl, Jutta; Liedl, Wolfgang; Wimmer, Heinz; Breitenbach, Michael; Weber, Manuela; Geltinger, Florian; Richter, Klaus; Rinnerthaler, Mark

doi:10.1002/yea.3286

Cited by 11 publications

(11 citation statements)

References 50 publications

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“…The dihydroethidium (DHE) assay was performed as described in [ 47 ]. The yeast strains were grown for 16h in liquid SC−glucose.…”

Section: Methodsmentioning

confidence: 99%

“…Cells were washed twice in 1 × PBS and 5 × 10 6 cells were resuspended in 200 μL 1 × PBS. GFP (green fluorescence protein) fluorescence was determined using an Anthos Zenyth 3100 plate reader (excitation: 485 nm; emission: 535 nm) as described [48]. The autofluorescence (cells without GFP expression) was subtracted from the signal reported.…”

Section: Reporter Measurementsmentioning

confidence: 99%

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Actin Cytoskeleton Regulation by the Yeast NADPH Oxidase Yno1p Impacts Processes Controlled by MAPK Pathways

et al. 2021

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Reactive oxygen species (ROS) that exceed the antioxidative capacity of the cell can be harmful and are termed oxidative stress. Increasing evidence suggests that ROS are not exclusively detrimental, but can fulfill important signaling functions. Recently, we have been able to demonstrate that a NADPH oxidase-like enzyme (termed Yno1p) exists in the single-celled organism Saccharomyces cerevisiae. This enzyme resides in the peripheral and perinuclear endoplasmic reticulum and functions in close proximity to the plasma membrane. Its product, hydrogen peroxide, which is also produced by the action of the superoxide dismutase, Sod1p, influences signaling of key regulatory proteins Ras2p and Yck1p/2p. In the present work, we demonstrate that Yno1p-derived H2O2 regulates outputs controlled by three MAP kinase pathways that can share components: the filamentous growth (filamentous growth MAPK (fMAPK)), pheromone response, and osmotic stress response (hyperosmolarity glycerol response, HOG) pathways. A key structural component and regulator in this process is the actin cytoskeleton. The nucleation and stabilization of actin are regulated by Yno1p. Cells lacking YNO1 showed reduced invasive growth, which could be reversed by stimulation of actin nucleation. Additionally, under osmotic stress, the vacuoles of a ∆yno1 strain show an enhanced fragmentation. During pheromone response induced by the addition of alpha-factor, Yno1p is responsible for a burst of ROS. Collectively, these results broaden the roles of ROS to encompass microbial differentiation responses and stress responses controlled by MAPK pathways.

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“…The dihydroethidium (DHE) assay was performed as described in [ 47 ]. The yeast strains were grown for 16h in liquid SC−glucose.…”

Section: Methodsmentioning

confidence: 99%

Section: Reporter Measurementsmentioning

confidence: 99%

Actin Cytoskeleton Regulation by the Yeast NADPH Oxidase Yno1p Impacts Processes Controlled by MAPK Pathways

et al. 2021

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“…The elutriation was performed as described earlier (Streubel et al 2018). At 28°C overnight cultures of BY4741 and the LD deficient QM strain were grown.…”

Section: Elutriationmentioning

confidence: 99%

The transfer of specific mitochondrial lipids and proteins to lipid droplets contributes to proteostasis upon stress and aging in the eukaryotic model system Saccharomyces cerevisiae

et al. 2019

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Originally Lipid droplets (LDs) were considered as being droplets for lipid storage only. Increasing evidence, however, demonstrates that LDs fulfill a pleiotropy of additional functions. Among them is the modulation of protein as well as lipid homeostasis. Under unfavorable pro-oxidative conditions, proteins can form aggregates which may exceed the overall proteolytic capacity of the proteasome. After stress termination LDs can adjust and support the removal of these aggregates. Additionally, LDs interact with mitochondria, specifically take over certain proteins and thus prevent apoptosis. LDs, which are loaded with these harmful proteins, are subsequently eliminated via lipophagy. Recently it was demonstrated that this autophagic process is a modulator of longevity. LDs do not only eliminate potentially dangerous proteins, but they are also able to prevent lipotoxicity by storing specific lipids. In the present study we used the model organism Saccharomyces cerevisiae to compare the proteome as well as lipidome of mitochondria and LDs under different conditions: replicative aging, stress and apoptosis. In this context we found an accumulation of proteins at LDs, supporting the role of LDs in proteostasis. Additionally, the composition of main lipid classes such as phosphatidylcholines, phosphatidylethanolamines, phosphatidylinositols, phosphatidylglycerols, triacylglycerols, ceramides, phosphatidic acids and ergosterol of LDs and mitochondria changed during stress conditions and aging.

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“…We investigated the alterations in myocardial CTS expression during aging, cardiac hypertrophy, and SCD. In particular, we focused on CTSB, CTSD, and CTSL, which are abundantly expressed in the human heart, and on their target proteins, namely p62, which is the major autophagic substrate and accumulates under lysosomal dysfunction [26], ATP synthase subunit c (ATPSC), which accumulates upon CTSD impairment [27], and αsynuclein (ASNC), which is degraded by CTSB and CTSL [28,29].…”

Section: Introductionmentioning

confidence: 99%

Myocardial cathepsin D is downregulated in sudden cardiac death

et al. 2020

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Cathepsins are the major lysosomal proteases that maintain intracellular homeostasis. Herein, we investigated the alterations in myocardial cathepsin expression during aging, cardiac hypertrophy, and sudden cardiac death (SCD). Cardiac tissue and blood were sampled from autopsy cases. Subjects were classified into three groups: SCD with cardiac hypertrophy (SCH), compensated cardiac hypertrophy (CCH), and control. Immunoblotting was performed for the major cardiac cathepsins and their targets: cathepsin B, D, and L (CTSB/D/L), p62, ATP synthase subunit c (ATPSC), and α-synuclein (ASNC). Immunohistochemical analysis and ELISA using serum samples were performed for CTSD. Cardiac CTSB and CTSD were upregulated with age (r = 0.63 and 0.60, respectively), whereas the levels of CTSL, p62, ATPSC, and ASNC remained unchanged. In age-matched groups, cardiac CTSD was significantly downregulated in SCH (p = 0.006) and CTSL was moderately downregulated in CCH (p = 0.021); however, p62, ATPSC, and ASNC were not upregulated in cardiac hypertrophy. Immunohistochemistry also revealed decreased myocardial CTSD levels in SCH, and serum CTSD levels were relatively lower in SCH cases. Overall, these results suggest that upregulation of cardiac CTSB and CTSD with age may compensate for the elevated proteolytic demand, and that downregulation of CTSD is potentially linked to SCH. OPEN ACCESS Citation: Kakimoto Y, Sasaki A, Niioka M, Kawabe N, Osawa M (2020) Myocardial cathepsin D is downregulated in sudden cardiac death. PLoS ONE 15(3): e0230375. https://doi.org/10.

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Behead and live long or the tale of cathepsin L

Cited by 11 publications

References 50 publications

Actin Cytoskeleton Regulation by the Yeast NADPH Oxidase Yno1p Impacts Processes Controlled by MAPK Pathways

Actin Cytoskeleton Regulation by the Yeast NADPH Oxidase Yno1p Impacts Processes Controlled by MAPK Pathways

The transfer of specific mitochondrial lipids and proteins to lipid droplets contributes to proteostasis upon stress and aging in the eukaryotic model system Saccharomyces cerevisiae

Myocardial cathepsin D is downregulated in sudden cardiac death

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