FEBS Press Awards
The FEBS Journal Richard Perham Prize 2021
The prize was awarded for the below outstanding paper published by Antonio Barbáchano, Alberto Muñoz and co-authors in The FEBS Journal in 2020. One of the senior authors, Dr Antonio Barbáchano (Instituto de Investigaciones Biomédicas 'Alberto Sols', Spanish National Research Council (CSIC), Madrid, Spain), will present a plenary lecture about this work at the IUBMB–FEBS–PABMB Congress on 9–14 July 2022.
Vitamin D differentially regulates colon stem cells in patient-derived normal and tumor organoids
Asunción Fernández-Barral, Alba Costales-Carrera, Sandra P. Buira, Peter Jung, Gemma Ferrer-Mayorga, María Jesús Larriba, Pilar Bustamante-Madrid, Orlando Domínguez, Francisco X. Real, Laura Guerra-Pastrián, Miguel Lafarga, Damián García-Olmo, Ramón Cantero, Luis Del Peso, Eduard Batlle, Federico Rojo, Alberto Muñoz and Antonio Barbáchano. FEBS J, 2020, 287: 53–72. doi:10.1111/febs.14998
Vitamin D deficiency has been linked to enhanced colorectal cancer (CRC) risk and mortality. Human colonic stem cells – known as crypt stem cells – are essential in gut homeostasis and their alteration is a feature of CRC. Alberto Muñoz, Antonio Barbáchano and colleagues generated a living-biobank of stem-cell-derived normal and tumor colon organoids from CRC patients. They show that vitamin D upregulates stemness-related genes and the undifferentiated phenotype in normal organoids, whereas it induces differentiation in tumor organoids. These findings uncover a regulatory role of vitamin D on crypt stem cells, with relevance to CRC development.
For more information about this award, please see The FEBS Journal Richard Perham Prize
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.
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 presented a plenary lecture about this work at the online 45th FEBS Congress on 3–8 July 2021, where he was officially presented with the prize.
For more information about this award, please see the FEBS Letters Award
Other FEBS Press Awards
For details on all FEBS awards, click here.