浙江中醫(yī)藥大學(xué)生命科學(xué)學(xué)院 Ivan Psakhye教授團(tuán)隊(duì)長(zhǎng)期招聘全職博士后，具體內(nèi)容詳見(jiàn)下方招聘信息“Opportunities for Postdocs in the laboratory of Ivan Psakhye – SUMO and Ubiquitin Pathways in Genome Stability”。

Opportunities for Postdocs in the laboratory of Ivan Psakhye – SUMO and Ubiquitin Pathways in Genome Stability

Employer:Zhejiang Chinese Medical University

Location:Hangzhou, Zhejiang, China

Salary:300,000 CNY annually plus competitive bonus determined by the level of experience, skill set and progress of the fellow.

Benefits:Medical insurance, campus food allowance and subsidized campus accommodation.

Starting date:October 1st, 2025. The starting date is flexible from October 1st2025, and applications will be reviewed on a rolling basis until the positions are filled.

Job Type: Postdoctoral

Employment: Full time

Duration: 3 years. The appointment is fully supported for 3 years, after which the position may be further extended if required.

Qualification:PhD

Research:

Our newly established laboratory at Zhejiang Chinese Medical University is currently seeking enthusiastic young scientists to join us as postdoctoral fellows. Our aim is to conduct fundamental mechanistic research with a focus on functional aspects related to the SUMO and ubiquitin pathways. Moreover, we have a general interest in DNA replication, DNA repair, sister chromatid cohesion, genome stability and chromatin biology, in particular if ubiquitin family proteins are involved. Because of the available tools for rapid and elegant genetic manipulation, budding yeast Saccharomyces cerevisiae is ideally suited for the mechanistic cell biology studies we conduct in the lab. To extend the significance of the findings made in yeast to a more universal level, key mechanistic insights will be validated also in mammalian cells.

Posttranslational modification (PTM) of proteins by attachment of ubiquitin (ubiquitylation) is best known for its function to label proteins for degradation by the proteasome. However, ubiquitylation plays non-proteolytic roles as well, e.g. for DNA repair, gene expression and signal transduction. Another member of the ubiquitin family, Small Ubiquitin-like Modifier (SUMO), functions primarily in the non-proteolytic (non-proteasomal) manner. It affects protein-protein interactions, interplays with the ubiquitin pathway, controls DNA repair, replication, sister chromatid cohesion and supports genome stability.

Ubiquitin typically targets individual proteins and high selectivity is provided by a plethora of ubiquitin-conjugating enzymes and ligases. Much less is known regarding how modification by the ubiquitin-related protein SUMO influences the function of its targets and how substrate specificity is achieved. Surprisingly, although thousands of proteins are modified by SUMO, only a handful of enzymes participate in the pathway. Moreover, although SUMO modification is essential for viability, mutants defective in SUMOylation of individual substrates typically lack deleterious phenotypes. We previously discovered that SUMOylation operates strategically different from ubiquitylation as it often targets entire groups of proteins that are spatially and functionally connected rather than individual substrates (Psakhye and Jentsch, Cell, 2012). In “protein-group modification” SUMO functions as intermolecular “glue” thereby stabilizing dynamic macromolecular protein complexes and concentrating activities. Thus, the traditional view that a single PTM on a given substrate mediates a specific function does not seem to apply for many SUMO modifications.

In our laboratory, we will focus on the principles of protein-group modification and its special requirements for specificity, formation, timing, and disassembly. We will expand the concept of protein-group SUMOylation with a focus on pathways relevant for cellular physiology, genome integrity in particular, and which are of medical importance. The broad scientific goal of the laboratory will be to advance the understanding of the general mechanisms and functions of the SUMO pathway, and its interplay with other PTM systems.

Below find the examples of the kind of research that we conduct for further reading:

·Psakhye and Jentsch, Cell, 2012. DOI: 10.1016/j.cell.2012.10.021

·Lu, Psakhye and Jentsch, Cell, 2014. DOI: 10.1016/j.cell.2014.05.048

·Psakhye, Castellucci and Branzei, Mol Cell, 2019. DOI: 10.1016/j.molcel.2019.08.003

·Psakhye and Branzei, Cell Rep, 2021. DOI: 10.1016/j.celrep.2021.109485

·Psakhye et al., Nat Struct Mol Biol, 2023. DOI: 10.1038/s41594-023-01064-x

A few things to consider:

·In our laboratory you can work on significant biological questions of general importance.

·Because our scientific interest is broad, you get in contact with a wide range of biological topics and have the choice of different projects.

·Our techniques and methods range from yeast genetics, protein biochemistry, cell biology, proteomics, microscopy to whole genome sequencing and advanced genetic and interaction screens.

·We have many opportunities for international collaborations and English is our working language.

Qualifications:

Applicants should have a strong interest in cell biology or molecular biology and high motivation to uncover the molecular mechanisms. We are conducting basic research and are mainly interested in discovering new cellular functions or principles rather than studying details.Postdoc candidates are expected with a record of successful research in the areas of molecular biology, cell biology, biochemistry, or genetics.

How to apply?

To apply, please forward a curriculum vitae, bibliography, and the names and addresses of referees to Prof. Ivan Psakhye: ivan.psakhye@zcmu.edu.cn

信息來(lái)源于網(wǎng)絡(luò)，如有變更請(qǐng)以原發(fā)布者為準(zhǔn)。

來(lái)源鏈接：

https://rczp.zcmu.edu.cn/apply/phoneMoreOne.action?keycode=0b5541ec-87d7-4809-bdf8-b177cc63dc0d

為防止簡(jiǎn)歷投遞丟失請(qǐng)抄送一份至：boshijob@126.com（郵件標(biāo)題格式：應(yīng)聘職位名稱+姓名+學(xué)歷+專業(yè)+中國(guó)博士人才網(wǎng)）