Journée Osez tous les Métiers (JOM) 2023 at the Génopode

If your child goes to school in the canton of Vaud, within the 7th to 9th year of school, the “Journée Oser tous les Métiers” concerns you.
It will be organized November 9, 2023.

Commun activities can be organized if enough persons are interested. An email will be sent to CIG and DBC members soon.

Should you have any question about the organisation, please contact Fabienne.Lammers@unil.ch.

Further information about activities organized by the UNIL can be found here:
https://www.unil.ch/egalite/fr/home/menuinst/evenements-et-formations/evenements/oser-tous-les-metiers-jom.html

Several positions are available in the De Paola lab at the Duke-NUS in Singapore (SG)

Research Fellow/Senior Research Fellow
https://www.nature.com/naturecareers/job/12805903/research-fellow-senior-research-fellow

Senior Research Associate
https://www.nature.com/naturecareers/job/12805900/senior-research-associate

Research Assistant/Senior Research Assistant
https://www.nature.com/naturecareers/job/12805895/research-assistantsenior-research-assistant

Further information: vincenzo.depaola@duke-nus.edu.sg

iScience.: co-auth.: M.Quadroni

iScience. 2023 Aug 29;26(10):107777.  doi: 10.1016/j.isci.2023.107777. eCollection 2023 Oct 20.

ER-trafficking triggers NRF1 ubiquitination to promote its proteolytic activation

Claire Chavarria 1Léa Zaffalon 1Sérgio T Ribeiro 1Mélanie Op 1Manfredo Quadroni 2Maria Sofia Iatrou 1Chloé Chapuis 1Fabio Martinon 1

Abstract

The transcription factor NRF1 resides in the endoplasmic reticulum (ER) and is constantly transported to the cytosol for proteasomal degradation. However, when the proteasome is defective, NRF1 escapes degradation and undergoes proteolytic cleavage by the protease DDI2, generating a transcriptionally active form that restores proteostasis, including proteasome function. The mechanisms that regulate NRF1 proteolytic activation and transcriptional potential remain poorly understood. This study demonstrates that the ER is a crucial regulator of NRF1 function by orchestrating its ubiquitination through the E3 ubiquitin ligase HRD1. We show that HRD1-mediated NRF1 ubiquitination is necessary for DDI2-mediated processing in cells. Furthermore, we found that deficiency in both RAD23A and RAD23B impaired DDI2-mediated NRF1 processing, indicating that these genes are essential components of the DDI2 proteolytic machinery. Our findings highlight the intricate mechanism by which the ER activates NRF1 to coordinate the transcriptional activity of an adaptation response in cells.

PLoS Biol.: co-auth.: B.Thorens

PLoS Biol. 2023 Sep 21;21(9):e3002308.  doi: 10.1371/journal.pbio.3002308. eCollection 2023 Sep.

Hyperglycemia increases SCO-spondin and Wnt5a secretion into the cerebrospinal fluid to regulate ependymal cell beating and glucose sensing

Francisco Nualart 1 2Manuel Cifuentes 3Eder Ramírez 2Fernando Martínez 1María José Barahona 2Luciano Ferrada 2Natalia Saldivia 1Ernesto R Bongarzone 4Bernard Thorens 5Katterine Salazar 1

Abstract

Hyperglycemia increases glucose concentrations in the cerebrospinal fluid (CSF), activating glucose-sensing mechanisms and feeding behavior in the hypothalamus. Here, we discuss how hyperglycemia temporarily modifies ependymal cell ciliary beating to increase hypothalamic glucose sensing. A high level of glucose in the rat CSF stimulates glucose transporter 2 (GLUT2)-positive subcommissural organ (SCO) cells to release SCO-spondin into the dorsal third ventricle. Genetic inactivation of mice GLUT2 decreases hyperglycemia-induced SCO-spondin secretion. In addition, SCO cells secrete Wnt5a-positive vesicles; thus, Wnt5a and SCO-spondin are found at the apex of dorsal ependymal cilia to regulate ciliary beating. Frizzled-2 and ROR2 receptors, as well as specific proteoglycans, such as glypican/testican (essential for the interaction of Wnt5a with its receptors) and Cx43 coupling, were also analyzed in ependymal cells. Finally, we propose that the SCO-spondin/Wnt5a/Frizzled-2/Cx43 axis in ependymal cells regulates ciliary beating, a cyclic and adaptive signaling mechanism to control glucose sensing.

Life Sciences Switzerland (LS2) – Deadline for abstract submission: Nov. 8, 2023

  • Deadline for abstract submission (posters and talks)8 November 2023
  • General registration: 10 January 2024

Register here: https://annual-meeting.ls2.ch/2024/registration

The program of this edition gathers an amazing panel of keynote speakersPr. Nicole King from the University of California, Berkeley (US), Dr. Samer Hattar from the National Institute of Mental Health (US), and Dr. Pavel Tomancakfrom the Max Planck Institute of Molecular Cell Biology and Genetics (DE) and Dr. Melina Schuh from the Max Planck Institute for Multidisciplinary Sciences (DE), who will give a keynote lecture at the Young Scientists’ Satellite.

But that’s not all, the 2024 edition of the LS2 Annual Meeting has many interesting things to offer:

Look at details of the program here and general information about abstracts, 3R Accreditation, Venue and more here.

PhD student positions open at the Max Planck Research School for Living Matter, Dortmund (DE)

The International Max Planck Research School for Living Matter (IMPRS-LM) is looking for talented and motivated PhD candidates of all nationalities with a background in MOLECULAR and CELL BIOLOGY, BIOCHEMISTRY, BIOPHYSICS, APPLIED and THEORETICAL PHYSICS, CHEMICAL BIOLOGY, STRUCTURAL BIOLOGY, SYSTEMS BIOLOGY and related fields.

Online applications are possible until October 19th, 2023.

Further information & application: https://www.imprs-lm.mpg.de/