Unravelling the mode of action of plant proteases

Hoorn, Renier A. L. van der; Rivas, Susana

doi:10.1111/nph.15156

Cited by 13 publications

(7 citation statements)

References 23 publications

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“…Clearly, further investigation is required to understand how PLCPs perceive stresses and signals and what is the downstream players in PLCP pathways. Sensitive and novel techniques, such as quantitative proteomics and labeling probes, were used to uncover protease substrates and function (Demir et al, 2018; van der Hoorn and Rivas, 2018), thereby may facilitate to advance our mechanical understanding to the function of plant PLCPs.…”

Section: Discussionmentioning

confidence: 99%

Role of Papain-Like Cysteine Proteases in Plant Development

et al. 2018

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Papain-like cysteine proteases (PLCP) are prominent peptidases found in most living organisms. In plants, PLCPs was divided into nine subgroups based on functional and structural characterization. They are key enzymes in protein proteolysis and involved in numerous physiological processes. In this paper, we reviewed the updated achievements of physiological roles of plant PLCPs in germination, development, senescence, immunity, and stress responses.

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Section: Discussionmentioning

confidence: 99%

Role of Papain-Like Cysteine Proteases in Plant Development

et al. 2018

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“…The UVR tolerance-response has been shown to be dose-dependent, and repair under UVR is a key element in D. tertiolecta resilience [18, 41–43]. Enzymes typically described in CD events in phytoplankton such as CL proteases are also implicated in managing the stress-response to UVR [18, 41], accordingly with some of the functions attributable to CLs in plants unrelated to CD [45]. The cleavage rate of CLs-reporter substrates was 10-fold lower than MCs-substrates.…”

Section: Discussionmentioning

confidence: 99%

Type II-Metacaspases are involved in cell stress but not in cell death in the unicellular green alga Dunaliella tertiolecta

Mata

Palma

García‐Gómez

et al. 2019

MIC

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Ultraviolet radiation (UVR; 280–400 nm) has a great impact on aquatic ecosystems by affecting ecophysiological and biogeochemical processes as a consequence of the global change scenario generated by anthropogenic activities. We studied the effect of PAR (P)+UVA (A)+UVB (B) i.e. PAB, on the molecular physiology of the unicellular green alga Dunaliella tertiolecta for six days. We assessed the relationship between the triggered UVR stress response and metacaspases and caspase-like (CL)activities, which are proteases denoted to participate in cell death (CD) in phytoplankton. UVR inhibited cell growth and in vivo chlorophyll a fluorescence but did not cause cell death. Western blot analyses reflected that Type-II metacaspases (MCs) are present and appear to be involved in UVR induced-cell stress but not in dark-induced CD in D. tertiolecta. Enzyme kinetics revealed that cleavage of the MCs-reporter substrates RVRR, QRR, GRR, LKR, HEK, and VLK was 10-fold higher than WEHD, DEVD, IETD, and LETD CLs-substrates. The lowest apparent Michaelis-Menten constants (KMap) corresponded to RVRRase (37.5 μM) indicating a high affinity by the RVRR substrate. The inhibition of enzymatic activities by using inhibitors with different target sites for hydrolyses demonstrated that from all of the R/ Kase activities only RVRRase was a potential candidate for being a metacaspase. In parallel, zymograms and peptide-mass fingerprinting analyses revealed the identities of such Rase activities suggesting an indirect evidence of possible natural physiological substrates of MCs. We present evidence of type II-MCs not being involved in CD in D. tertiolecta, but rather in survival strategies under the stressful irradiance conditions applied in this study.

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“…Proteolytic processing often regulates protein activity and creates variation in a protein's function. This has been suggested by phylogenetic and functional studies in all kingdoms of life, including viruses [15], plants [16], and animals [17]. Not surprisingly, proteases are used to regulate function and create functional variety in the VEGF family and can be regarded as signaling molecules [18].…”

Section: Figurementioning

confidence: 96%

The Proteolytic Activation of Vascular Endothelial Growth Factors

Künnapuu¹,

Bokharaie²,

Jeltsch³

2021

Preprint

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Specific proteolytic cleavages turn on, modify, or turn off the activity of vascular endothelial growth factors (VEGFs). Proteolysis is most prominent among the lymphangiogenic VEGF-C and VEGF-D, which are synthesized as precursors that need to undergo enzymatic removal of their C- and N-terminal propeptides before they can activate their receptors. The activating cleavage of VEGF-C is mediated by at least five different proteases: plasmin, ADAMTS3, prostate-specific antigen, cathepsin D, and thrombin. All of these proteases except for ADAMTS3 can also activate VEGF-D. Processing by different proteases results in distinct forms of the "mature" growth factors, which differ in affinity and receptor activation potential. The “default” VEGF-C-activating enzyme ADAMTS3 does not activate VEGF-D and therefore, VEGF-C and VEGF-D do function in different contexts. VEGF-C itself is also regulated in different contexts by different proteases. During embryonic development, ADAMTS3 activates VEGF-C. In contrast, thrombin and plasmin likely activate VEGF-C/-D during tissue injury-induced lymphangiogenesis, and PSA and cathepsin D perhaps during tumor-associated pathological lymphangiogenesis. Additionally, cathepsin D from saliva might activate latent VEGF-C/-D upon wound licking, thereby accelerating healing. Similar to tyrosine kinase receptors and VEGFs themselves, these activating proteases could be targeted to modulate angiogenesis and lymphangiogenesis in relevant diseases.

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Unravelling the mode of action of plant proteases

Cited by 13 publications

References 23 publications

Role of Papain-Like Cysteine Proteases in Plant Development

Role of Papain-Like Cysteine Proteases in Plant Development

Type II-Metacaspases are involved in cell stress but not in cell death in the unicellular green alga Dunaliella tertiolecta

The Proteolytic Activation of Vascular Endothelial Growth Factors

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