Open Positions

The nuclear pore complex (NPC) is a large cylindrical structure with multiple copies of over 30 different proteins named nucleoporins (NUPs). The NPC is embedded in the nuclear envelope (NE) at fusion sites of the inner and outer nuclear membrane where it facilitates nuclear-cytoplasmic transport of RNA and proteins. NPCs assemble in the intact nuclear envelope (interphase human cells or yeast cells with a closed mitosis) by an inside-out mechanism. NUPs become deposited from within the nucleus to the inner nuclear membrane, deform this membrane and eventually the inner and outer nuclear membranes fuse. We recently have identified with Brr6 and Brl1 two conserved integral membrane proteins that may play a role in nuclear membrane fusion during NPC biogenesis.

In this project we will study NPC biogenesis using budding yeast and human cells as model systems. The PhD student will use biochemical approaches (Brr6 and Brl1 reconstitution into liposomes), super resolution microscopy (MinFlux), electron microscopy, CRISPR/Cas9 technology and live cell imaging to study NPC assembly.

Highly motivated PhD students with a background in biochemistry, cell biology or molecular biology should apply. Successful candidates will be part of an international team of PhD students and postdocs that works at the forefront of scientific research. The PhD student will be a member of the Heidelberg Biosciences International Graduate School (HBIGS) (http://www.hbigs.uni-heidelberg.de). 

The PhD position is funded in the first instance for 3 years

Please send applications to E. Schiebel (schiebel.elmar@zmbh.uni-heidelberg.de).

Relevant recent publications:

1          Zhang, W. et al. Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis. J Cell Biol217, 877-894 (2018). 

2          Zhang, W. et al. A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis. Open biology doi: 10.1098/rsob.210250.  (2021). 

3          Vitale, J., Khan, A., Neuner, A. & Schiebel, E. A perinuclear alpha-helix with amphipathic features in Brl1 promotes NPC assembly. Mol Biol Cell 33, ar35 (2022). https://doi.org:10.1091/mbc.E21-12-0616

from November 1, 2023

we offer a Hiwi Position for lab work (insect cell culturing)

Flexible working time, 8 - 10 hours per week

Prerequisites:

• Experience in tissue culture work

• Must be available for at least 1 year

Please apply to E. Schiebel: schiebel.elmar@zmbh.uni-heidelberg.de

My laboratory at the ZMBH, University of Heidelberg, is offering Master projects in the following areas:

The structure and function of gamma-tubulin complexes.  Gamma-tubulin complexes assemble microtubules from tubulin subunits. Microtubules have essential functions for chromosome segregation in mitosis and meiosis, fertility, transport process in particularly in neurons. Drugs such as Taxol that target tubulin are broadly used in cancer therapy. Gamma-tubulin complexes regulate the spatial and temporal formation of microtubules. In this project we determine the structure of gamma-tubulin complexes by Cryo-EM. We will also analyse how gamma-tubulin complexes interact with microtubule polymerases.

Centrosome duplication and centriole-centrosome conversion. Centrosomes are the main microtubule organizing centres in human cells. They only duplicate once per cell cycle. Misregulation of centrosome duplication triggers a p53 response and G1 arrest. This safeguard mechanism is bypassed in cancer cells. After duplication in S phase centrosomes convert into mature centrosomes. Here we analyse the molecular mechanism of this conversion process.

Centrosome cohesion. The two centrosomes of a cell are linked together into one unit from G1 until G2 phase. At the beginning of mitosis this linkage is resolved by the kinase NEK2. Here we will study molecular mechanisms of this linkage, the structure of the linker and functional consequences if centrosome cohesion fails.

Nuclear pore complex biogenesis and spindle pole body duplication. Nuclear pore complexes and the yeast spindle pole body (SPB; yeast microtubule organizing centre) are both embedded in the double membrane of the nuclear envelope. Here we aim to understand how large protein assemblies become inserted into the nuclear envelope and how the inner and outer nuclear envelopes fuse during this embedding process.

During the 6-month master project, you will receive a Student Assistant Contract (Hiwi contract).

Please send applications with a short motivation letter, CV, bachelor transcripts and the name of one referee to Prof. Dr. E. Schiebel (schiebel.elmar@zmbh.uni-heidelberg.de).