Prof. Dr. Martin Spiess

Biozentrum
University of Basel
Klingelbergstrasse 50 / 70
CH - 4056 Basel
Biozentrum, Room 577A Phone: +41 61 267 21 64
Email: martin.spiess-at-unibas.ch
Curriculum Vitae

Administrative Assistant

Maja Heckel
Biozentrum, Room 508
Phone: +41 61 267 21 51
Fax: +41 61 267 21 48
Email: maja.heckel-at-unibas.ch

Brigitte Olufsen
Biozentrum, Room 510
Phone: +41 61 267 21 45
Fax: +41 61 267 21 48
Email: brigitte.olufsen-at-unibas.ch

Research group Martin Spiess

Membrane proteins and their transport in the cell

How are membrane proteins correctly assembled in the cell membrane and transported through the complex network of organelles in the cell? Errors in protein transport may result in disease.

Colonies of yeast cells.

All of our cells are surrounded by a lipid membrane, just as all the organelles within the cell are separated from each other by membranes. These membranes consist of lipids and membrane proteins that are first assembled in the membrane of the endoplasmic reticulum (ER), a network spanning the entire cell. Membrane proteins are then sorted and transported to their intended organelles.

Folding of membrane proteins

Just how proteins fold into the lipid membrane is determined by their amino acid sequence. Our goal is to understand the process of protein folding and orientation in cell cultures, and in yeast cells as a model organism.

Membrane transport

Protein transport between organelles typically involves formation of a vesicle containing the protein to be transported from the membrane. The vesicle then fuses with the target organelle. Our research focuses on this mechanism and its regulation; in particular, we are looking at the uptake of proteins at the cell surface and their recycling.

Diabetes insipidus

Although the hormone vasopressin itself is not a membrane protein, it is also transported from the ER to the cell surface. Mutations that disrupt its export cause the cells to die and result in diabetes insipidus, a rare metabolic disorder. We have discovered that these mutations give rise to protein aggregates, similar to those seen in neurological conditions such as Alzheimer's disease, and we are investigating how this happens.