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The past few decades have seen increasingly rapid advances in the field of sustainable energy technologies. As a new bio- and eco-friendly energy source, enzymatic biofuel cells (EBFCs) have garnered significant research interest due to their capacity to power implantable bioelectronics, portable devices, and biosensors by utilizing biomass as fuel under mild circumstances. Nonetheless, numerous obstacles impeded the commercialization of EBFCs, including their relatively modest power output and poor long-termstability of enzymes. To depict the current progress of EBFC and address the challenges it faces, this review traces back the evolution of EBFC and focuses on contemporary advances such as newly emergedmulti or single enzyme systems, various porous framework-enzyme composites techniques, and innovative applications. Besides emphasizing current achievements in this field, fromour perspective part we also introduced novel electrode and cell design for highly effective EBFC fabrication.We believe this review will assist readers in comprehending the basic research and applications of EBFCs as well as potentially spark interdisciplinary collaboration for addressing the pressing issues in this field. [ABSTRACT FROM AUTHOR]

Ubiquitination plays important and diverse roles in modulating protein functions. As a C2-WW-HECT-type ubiquitin ligase, Smad ubiquitination regulatory factor 1 (Smurf1) commonly serves to regulate ubiquitin-dependent protein degradation in a number of signaling pathways. Here, we report a novel function of Smurf1 in regulating Wnt/β-catenin signaling through targeting axin for nonproteolytic ubiquitination. Our data unambiguously demonstrate that Smurf1 ubiquitinates axin through Lys 29 (K29)-linked polyubiquitin chains. Unexpectedly, Smurf1-mediated axin ubiquitination does not lead to its degradation but instead disrupts its interaction with the Wnt coreceptors LRP5/6, which subsequently attenuates Wnt-stimulated LRP6 phosphorylation and represses Wnt/β-catenin signaling. The inhibitory function of Smurf1 on Wnt/β-catenin signaling is further evidenced by analysis with Smurf1 knockout murine embryonic fibroblasts. We next identified K789 and K821 in axin as the ubiquitination sites by Smurf1. Consistently, Smurf1 could neither disrupt the interaction of an axinK789/821R double mutant with LRP5/6 nor attenuate the phosphorylation of LRP6 in axinK789/821R-expressing cells. Collectively, our studies uncover Smurf1 as a new regulator for the Wnt/β-catenin signaling pathway via modulating the activity of axin. [ABSTRACT FROM AUTHOR]