FEBS Press Awards
The FEBS Open Bio Article Prize 2021
We are pleased to announce that the inaugural 2021 FEBS Open Bio Article Prize will be awarded to Dr Arpit Katiyar (formerly of Yamaguchi University School of Medicine, Ube, Japan) as the first author of the following outstanding paper:
HSF1 is required for induction of mitochondrial chaperones during the mitochondrial unfolded protein response
Arpit Katiyar, Mitsuaki Fujimoto, Ke Tan, Ai Kurashima, Pratibha Srivastava, Mariko Okada, Ryosuke Takii and Akira Nakai. FEBS Open Bio, 2020, 10(6):1135–1148. doi: 10.1002/2211-5463.12863
The mitochondrial unfolded protein response (UPRmt) is characterized by the transcriptional induction of mitochondrial chaperone and protease genes in response to impaired mitochondrial proteostasis. In this article, the authors showed that the heat shock transcription factor HSF1 is required for activation of mitochondrial chaperone genes in mouse embryonic fibroblasts during impaired mitochondrial proteostasis. The authors also observed that HSF1 binds constitutively to mitochondrial chaperone gene promoters and it supports the maintenance of mitochondrial function. The findings in this award-winning paper suggest that HSF1 is required for induction of mitochondrial chaperones during the UPRmt.
The winning article was selected during a meeting hosted by the journal’s editorial manager Duncan Wright by a jury comprised of three members of the journal’s Editorial Board: Stuart Ferguson (Oxford), Takashi Gojobori (Mishima), and Alex Wlodawer (Frederick).
Dr Katiyar has been invited to submit an abstract on his current work for presentation at the 46th FEBS Congress to be held in Lisbon, Portugal, 9–14 July 2022.
For more information about this award, please see the FEBS Open Bio Article Prize.
The FEBS Letters Award 2020
FEBS Letters is pleased to announce that the FEBS Letters Award 2020 will be presented to Dr Tim Bartels (UK Dementia Research Institute at UCL) for his outstanding paper:
Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces
Matteo Rovere, John B. Sanderson, Luis Fonseca-Ornelas, Dushyant S. Patel and Tim Bartels. FEBS Lett, 2018, 592: 1464–1472. doi:10.1002/1873-3468.13047
α-Synuclein is a neuronal protein of unknown physiological function. Pathological aggregates of a-synuclein are a hallmark of Dementia with Lewy Bodies (DLB), Parkinson’s disease (PD) and Multiple System Atrophy.
The lab of Tim Bartels found that a soluble form of α-synuclein exists as an α-helically folded tetramer. This soluble form of α-synuclein is not prone to aggregation and its folding is favored by interaction with lipid bilayers, which appear to act as molecular chaperones modulating the conformational space of the folding protein. The authors propose a scenario whereby α-synuclein is present in two conformational pools: one of them aggregation‐prone, soluble and unfolded, and the other α‐helical and aggregation‐resistant. Imbalances in the relative amounts of protein in these two pools could favor nucleation events and subsequent aggregation.
The award-winning article is selected by a special committee, formed by appointed members of the Editorial Board, plus one external member. The Award Committee members were: Laszlo Nagy (Orlando), Britta Brügger (Heidelberg), Nicola Gray (Edinburgh), Daniela Ruffell (Editorial Office) and Michael Brunner (Associate Managing Editor), Chair.
Dr Bartels will present a plenary lecture about this work at the online 45th FEBS Congress on 3–8 July 2021, where he will be officially presented with the prize.
For more information about this award, please see the FEBS Letters Award
The FEBS Journal Richard Perham Prize 2020
The prize was awarded for the below outstanding paper published by Kazunori Mori and co-authors in The FEBS Journal in 2019. The senior author, Dr Motoko Shibanuma (Showa University School of Pharmacy, Tokyo, Japan), will present a plenary lecture about this work at the online 45th FEBS Congress on 3–8 July 2021.
A mitochondrial ROS pathway controls matrix metalloproteinase 9 levels and invasive properties in RAS‐activated cancer cells
Kazunori Mori, Tetsu Uchida, Toshihiko Yoshie, Yuko Mizote. Fumihiro Ishikawa, Masato Katsuyama and Motoko Shibanuma
FEBS J, 2019, 286: 459–478. doi:10.1111/febs.14671
Matrix metalloproteinases (MMPs) are a group of tissue‐remodeling enzymes that have been linked to a variety of pathophysiological processes, including cancer metastasis. In this study, the authors provided new insights into the regulation of MMP9. They showed that the molecular adaptor protein HIC‐5 suppresses the activation of NADPH oxidase 4 (NOX4), leading to downregulation of mitochondrial ROS levels, which in turn destabilizes MMP9 mRNA. They further demonstrated that this regulatory axis operates specifically in cancer cells harboring oncogenic mutations in H‐ or K‐ras, potentially unveiling a new therapeutic avenue for cancer therapy based on inhibition of MMPs.
For more information about this award, please see The FEBS Journal Richard Perham Prize
Other FEBS Press Awards
For details on all FEBS awards, click here.