closes
10
December

Postdoctoral fellow

Laboratory of Protein Metabolism in Development and Aging

Location: Warsaw, a vibrant city with an international academic research environment. International Institute of Molecular and Cell Biology (www.iimcb.gov.pl) - one of the most dynamic and top ranked Polish research institutes.

Job description: Laboratory of Protein Metabolism in Development and Aging is seeking highly motivated and talented Postdoc to join young team investigating the protein homeostasis in development and aging. We use both genetic, molecular and biochemical approaches, primarily in the C. elegans, to study proteolytic networks. Postdoc fellowship is funded in frame of National Science Centre OPUS grant.

Summary: Organismal development or environmental stimuli challenge the homeostatic protein balance (proteostasis) of individual cells, tissues or the entire organism. The ubiquitin proteasome system (UPS) is a key determinant of proteostasis as it regulates the turnover of damaged proteins supporting cellular protein homeostasis and thereby maintains the proteome during stress and aging. Our long-term objective is to understand the mechanistic and developmental aspects of protein degradation pathways defined by combinations of particular ubiquitin ligases (E3). The identification of stress and aging-induced signals that coordinate the interplay between specific E3s will offer intriguingly new mechanistic insights how proteolytic networks are fine-tuned to maintain the cellular proteome and support development and longevity.

Qualifications:
• PhD (or be close to completion) in Molecular Biology, Cell Biology, Protein Chemistry, Genetics or a related discipline;
• experience in C. elegans or cell culture is an advantage;
• experience in molecular biology, biochemistry and genomic engineering is an advantage;
• good writing and oral communication skills in English, and competence in scientific writing.

How to apply:
Please send your application including CV, motivation letter and the list of publications to the e-mail address: This email address is being protected from spambots. You need JavaScript enabled to view it., until 10th December 2017. Thanking all applicants for their interest, we will contact only selected candidates for an interview. Please include in your application the following statement: “In accordance with the personal data protection act from the 29th of August 1997, I hereby agree to process and to store my personal data by the Institution for recruitment purposes”. The recruitment procedure fulfils the National Science Centre’s regulations on granting the scholarships to young scientists.

Selected publications:
Riga T*, Pokrzywa W*, Kevei E, Akyuz M, Vishnu Balaji, Svenja Adrian, Hoehfeld J, Hoppe T. (2017). The ubiquitin ligase CHIP integrates proteostasis and aging by regulation of insulin receptor turnover. Cell. 169: 470-482.

Ackermann L., Schell M., Pokrzywa W., Gartner A., Schumacher B., Hoppe T. (2016). E4 ubiquitin ligase specific degradation hubs coordinate DNA double strand break repair and apoptosis. Nat Struct Mol Biol. 23: 995-1002

Kaushik S, and Cuervo AM (2015). Proteostasis and aging. Nat Med. 21, 1406-15

Frumkin A, Dror S, Pokrzywa W, Bar-Lavan Y, Karady I, Hoppe T, Ben-Zvi A. (2014). Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegans. Front Mol Biosci., doi: 10.3389
van Oosten-Hawle P, and Morimoto RI (2014). Organismal proteostasis: role of cell-nonautonomous regulation and transcellular chaperone signaling. Genes & Dev. 28: 1533-43

Segref A, Kevei E, Pokrzywa W, Mansfeld J, Schmeisser K, Livnat-Levanon N, Ensenauer R, Glickman M.H, Ristow M, Hoppe T. (2014). Pathogenesis of human mitochondrial diseases is modulated by reduced activity of the ubiquitin/proteasome-system. Cell Metab. 4:642-652

Pokrzywa W. and Hoppe T. (2013). Chaperoning myosin assembly in muscle formation and aging. Worm. 2:e25644

Gazda L*, Pokrzywa W*, Hellerschmied D, Loewe T, Forné I, Mueller-Planitz F, Hoppe T, Clausen T. (2013). The myosin chaperone UNC-45 is organized in tandem modules to support myofilaments formation in C. elegans. Cell. 1, 183-195.

Kuhlbrodt K, Janiesch PC, Kevei E, Segref A, Barikbin R, and Hoppe T (2011). The Machado-Joseph disease deubiquitylase ATX-3 couples longevity and proteostasis. Nat Cell Biol. 13, 273-281.