meinecke-lab

Welcome to the Meinecke Lab

We just published that the ERAD pore formed by Hrd1 is the first ubiquitin-gated channel ever described.
Congrats Niels and Vedran, we are very proud of you.

Meinecke Lab

Prof. Dr. Michael Meinecke | CV

University Medical Center Göttignen
Department of Cellular Biochemistry
Humboldtallee 23
37073 Göttingen
Germany

Tel. Office: +49 (0)551 39 8189
Tel. Lab: +49 (0)551 39 8188

E-Mail: michael.meinecke[at]med.uni-goettingen.de

Present Group Members

PostDocs

Dr. Mariam Barbot | Mari did her PhD in our group, identifying Mic10 as a major regulator of inner mitochondrial membrane morphology. She now is a joined PostDoc with the Jakobs group and still interested in how Mic10 works on a molecular level.

Dr. Daryna Tarasenko | After doing her PhD with us Daryna now is a PostDoc in our group. She works towards a comprehensive understanding of how cristae junctions are formed in the mitochondrial inner membrane.

PhD students

Mausumi Ghosh | Mausumi joined our group in 2019. During her PhD thesis she will characterize protein translocation pores using high-resolution single-channel electropyhsiology.

Barbora Knotková | Barbora joined our lab most recently as a PhD student. She works towards a reconstitution and functional characterization of membrane contact sites

Indrani Mukherjee | In her PhD thesis Indrani is working on the details of MICOS dependent membrane remodeling.

Fereshteh Sadeqi | Fereshteh is a PhD student in the lab. She is interested in the molecular details of protein-lipid interactions.

Staff

Tanja Gall | Tanja is our technician.

Alumni

Dr. Niels Denkert | Niels did his PhD thesis and a PostDoc our group. He is now on his way to become a patent laywer.

Dr. Benjamin Kroppen | Ben did his PhD thesis in our group and worked on the cooperativity of proteins and lipids in endocytosis.

We are always interested in recruiting highly motivated and creative PostDocs and PhD students (also Bachelor and Master students are welcome) to study the fascinating molecular organization of biological membranes. Our lab takes an interdisciplinary approach to this topic, employing biophysical, biochemical and cell biological techniques. If you are interested in joining the group or have further questions do not hesitate to contact Michael Meinecke.

Curriculum Vitae

Since 2017 | Professor for Membranebiochemistry at the Department of Biochemistry of the University of Göttingen
Since 2016 | Project leader, Collaborative Research Center 1190 (SFB 1190) 'Compartmental Gates and Contact Sites in Cells'
2013 - 2017 | Jun.-Professor for Molecular Membrane Biochemistry
Since 2013 | Project leader, Reserach Unit 1905 (Forschergruppe 1905) 'Structure and Function of the Peroxisomal Translocon (PerTrans)'
Since 2013 | Project leader, Collaborative Research Center 803 (SFB 803) 'Functionality controlled by organization in and between membranes'
Since 2012 | Associated research group of the European Neuroscience Institute Göttingen
Since 2012 | Independent group leader at the Department of Biochemistry of the University of Göttingen
2008 - 2011 | Postdoctoral fellow at the MRC – Laboratory of Molecular Biology, Cambridge, UK
2004 - 2007 | PhD thesis, Department of Biophysics, University of Osnabrück
2003 | Visiting scientist in the labs of Prof. Dr. Janet M. Wood and Prof. Dr. Ross Hallet, University of Guelph, Canada
1999 - 2003 | Studies of Biology and Biophysics at the University of Osnabrück

Research

Mitochondria are surrounded by two membranes. The inner membrane is highly folded and displays a complex and beautiful morphology that puzzles cell biologists for decades. We have identified proteins that shape the mitochondrial inner membrane and aim to understand how they work on a molecular level.
Read more
Over half of the cellular proteins have to cross at least one membrane to reach their workplace. Protein translocation pores have been found in virtually all cellular membranes. We are interested in identifying new pores and to understand their physiological regulation.
Read more
Clathrin mediated endocytosis is a specialised form of vesicle budding from the plasma membrane, important for the internalisation of external cargo molecules or membrane receptors. Over the course of a minute the flat plasma membrane deforms into a highly curved clathrin coated vesicle. We study proteins involved in this process and are interested in the biophysical details of protein-dependent membrane deformation.
Read more

Mitochondrial Inner Membrane Morphology

Biological membranes exhibit function-related shapes, leading to a plethora of complex and beautiful cell and cell organellar morphologies. Most if not all of these structures have evolved for a particular physiological reason. The shapes of these structures are formed by physical forces that operate on membranes. To create particular shaped cells and cell organelles, membranes must undergo deformations which are determined by the structure and elasticity of the membrane and this process is most probable driven by proteins, lipids and/or interplay of both. Therefore, an important question of current cell biology in conjunction with physics and mathematics is to elucidate the functional cause for these different membrane morphologies as well as how they are formed.
One of the most peculiar membrane shapes is observed in mitochondria. These organelles are surrounded by two membranes and especially the convoluted inner membrane displays a complex ultra-structure. A molecular understanding of how this membrane is shaped is missing to a large extent. Major structure giving elements of the inner membrane are the so-called cristae junctions. This short, tubular membrane segments connect the flat inner boundary membrane with the morphological dynamic cristae membranes. Cristae junctions are rather uniform with inner diameters between 15 – 35 nm and hence display high degrees of membrane curvature. They are thought to be important for cellular physiology as they help to maintain specific protein composition of inner membrane sub-domains. They are further implicated to play a major role during the intrinsic apoptotic pathway. Here, cristae junctions need to open to mobilize cytochrome c that is usually stored in intra-cristae spaces. Understanding how cristae junctions are formed and maintained or in other words, unraveling the molecular mechanisms of membrane remodeling at cristae junctions, is therefore of utmost importance. Unlike membrane remodeling in classical curvature-dependent processes like clathrin-mediated endocytosis, cristae junctions are most likely shaped by integral membrane proteins. At least some of these proteins are likely to be found within the MICOS complex (mitochondrial contact site and cristae organizing system). In recent years we were able to identify two inner membrane proteins that are part of the MICOS, with the ability to bend membranes at cristae junctions (check out our papers here, here and here).