Applications and platforms in digitalisation of wind farm O&M – community feedback and survey results

Abstract Achieving performance optimisation and cost savings by advanced data analysis techniques and improved digital communication is a significant focus of wind farm operators and research organisations often framed under the terms IoT or Industry 4.0. Within the research project ‘ModernWindABS’, Fraunhofer IEE has conducted a twofold approach to identify new applications using modern methods that will innovate operation and maintenance processes. Based on a systematic structure of O&amp;M processes and mathematic methods, innovative applications were identified and evaluated in expert workshops. Separately a survey among wind industry professionals with the focus on innovative applications through digital platforms has been conducted in partnership with German industry associations. From both approaches, applications, that enable failure risk monitoring, turn out as the highest priorities from the professionals consulted. Additionally, the survey results yield insights on participants’ expectations on benefits and financial contribution per organisational role and preferences regarding the platform setup and points out gaps between these expectations and current platform service designs. It further identifies the main barriers to the broader use of platforms, of which organisational and legal obstacles seem to outweigh technical problems.</jats:p

A Ca(2+) signaling pathway regulates a K(+) channel for low-K response in Arabidopsis

Nutrient sensing is critical for plant adaptation to the environment. Because of extensive farming and erosion, low content of mineral nutrients such as potassium (K(+)) in soils becomes a limiting factor for plant growth. In response to low-K conditions, plants enhance their capability of K(+) uptake through an unknown signaling mechanism. Here we report the identification of a Ca(2+)-dependent pathway for low-K response in Arabidopsis. We are not aware of any other example of a molecular pathway for a nutrient response in plants. Earlier genetic analyses revealed three genes encoding two Ca(2+) sensors (CBL1 and CBL9) and their target protein kinase (CIPK23) to be critical for plant growth on low-K media and for stomatal regulation, indicating that these calcium signaling components participate in the low-K response and turgor regulation. In this study, we show that the protein kinase CIPK23 interacted with, and phosphorylated, a voltage-gated inward K(+) channel (AKT1) required for K(+) acquisition in Arabidopsis. In the Xenopus oocyte system, our studies showed that interacting calcium sensors (CBL1 and CBL9) together with target kinase CIPK23, but not either component alone, activated the AKT1 channel in a Ca(2+)-dependent manner, connecting the Ca(2+) signal to enhanced K(+) uptake through activation of a K(+) channel. Disruption of both CBL1 and CBL9 or CIPK23 gene in Arabidopsis reduced the AKT1 activity in the mutant roots, confirming that the Ca(2+)-CBL-CIPK pathway functions to orchestrate transporting activities in planta according to external K(+) availability

A protein phosphorylation/dephosphorylation network regulates a plant potassium channel

Potassium (K+) is an essential nutrient for plant growth and development. Plants often adapt to low K+ conditions by increasing their K+ uptake capability. Recent studies have led to the identification of a calcium signaling pathway that enables plants to act in this capacity. Calcium is linked to two calcineurin B-like calcium sensors (CBLs) and a target kinase (CBL-interacting protein kinase 23 or CIPK23) that, in turn, appears to phosphorylate and activate the potassium channel, Arabidopsis K+ transporter 1 (AKT1), responsible for K+ uptake in roots. Here, we report evidence that this regulatory mechanism is more elaborate than earlier envisaged. The recently described pathway is part of an extensive network whereby several CBLs interact with multiple CIPKs in the activation of the potassium channel, AKT1. The physical interactions among the CBL, CIPK, and AKT1 components provide a mechanism for specifying the members of the CBL and CIPK families functional in AKT1 regulation. The interaction between the CIPKs and AKT1 was found to involve the kinase domain of the CIPK component and the ankyrin repeat domain of the channel. Furthermore, we identified a 2C-type protein phosphatase that physically interacts and inactivates the AKT1 channel. These findings provide evidence that the calcium-sensitive CBL and CIPK families together with 2C-type protein phosphatases form a protein phoshporylation/dephosphorylation network that regulates the AKT1 channel for K+ transport in plants