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Blanchard, L.

Publications and source records attributed to Blanchard, L..

2 recordsLinked to original sources

Large and persistent social risks to forest carbon projects

Despite the popularity of carbon credits as a tool to offset greenhouse gas emissions, there are growing concerns over whether their climate mitigation claims are robust. Most attention has focused on natural risks to forest carbon projects, such as wildfire, while social risks (e.g., those driven by fraud, mismanagement, and land conflicts) remain largely unquantified. Here we analyze 244 forest-based carbon projects to assess the vulnerability of the voluntary carbon market to social risks and find that projects systematically underestimate their risk of failure. Even under optimistic assumptions, projects are roughly twice as likely to fail within 25 years as their self-assessed risk implies over a 100-year horizon. Projecting these trends forward, we show that credits issued to failed projects could exceed the reserves registries hold to mitigate these risks within 1-2 decades. Overall, our results suggest stronger mechanisms and reserves are needed to ensure carbon credits deliver the promised climate benefits.

ecology↗

Redox regulation by the CDSP32 thioredoxin of ATP-synthase activity and enzymatic antioxidant network in Solanum tuberosum

Plant thioredoxins (TRXs) form a complex family involved in numerous metabolic and signalling pathways, such as the regulation of photosynthetic metabolism in relation with light conditions. The atypical CDSP32, chloroplastic drought-induced stress protein of 32 kDa, TRX includes two TRX-fold domains, one of which has an atypical redox-active HCGPC motif, and has been initially reported to participate in responses to oxidative stress as an electron donor to peroxiredoxins and methionine sulfoxide reductases. Here, we further characterized potato lines modified for CDSP32 expression to clarify the physiological roles of the TRX. Upon high salt treatments, modified lines displayed changes in the abundance and redox status of CDSP32 antioxidant partners, and exhibited sensitivity to NaHCO3, but not to NaCl. In non-stressed plants overexpressing CDSP32, a lower abundance of photosystem II PsbO and D1 subunits and ATP-synthase {gamma} subunit was noticed. The CDSP32 co-suppressed line showed altered chlorophyll a fluorescence induction and modified regulation of the plastidial ATP-synthase activity during dark/light and light/dark transitions, revealing the involvement of CDSP32 in the control of the photosynthetic machinery. In agreement with the previously reported interaction in planta between CDSP32 and the ATP-synthase {gamma} subunit, our data show that CDSP32 participates in the regulation of the transthylakoid membrane potential. Consistently, modeling of protein complex 3-D structure indicates that the CDSP32 TRX constitutes a suitable partner of ATP-synthase {gamma} subunit. We discuss the roles of CDSP32 in chloroplast redox homeostasis through the regulation of both photosynthetic activity and enzymatic antioxidant network.

plant biology↗