Loose Group
Self-Organization of Protein Systems
How are nanometer-sized proteins able to perform complex cellular functions on a much larger scale? The Loose group seeks to understand how proteins self-organize into dynamic spatiotemporal patterns using an in vitro reconstitution approach.
Dynamic protein assemblies play a central role in organizing cells in space and time. They emerge from complex interactions among many cellular components, yet a mechanistic understanding of how these interactions give rise to large-scale, dynamic organization is often still lacking. In the Loose group, we combine protein biochemistry, biomimetic membrane systems, quantitative fluorescence microscopy, and image analysis to uncover the emergent properties of biochemical networks that underlie cellular organization.
Our research focuses on three interconnected areas: (1) bacterial cell division, where we dissect how the FtsZ cytoskeleton and its regulators generate the dynamic Z-ring; (2) regulatory networks of small GTPases, where we rebuild minimal Rab signaling circuits to understand how membrane identities emerge and are maintained; and (3) the diversification of protein systems during evolution. By bridging bacterial and eukaryotic systems, integrating structural and evolutionary approaches, and combining experiments with theory, our work aims to identify universal design principles of protein self-organization that govern cellular organization across evolution.
Group Leader
Administrative Support
Team
Current Projects
Self-organization of the bacterial cell division machinery | Emergent properties of small GTPase networks
Publications
Wilmes S, Tönjes J, Drechsler M, Ruf A, Schäfer JH, Lürick A, Januliene D, Apelt S, Di Iorio D, Wegner SV, Loose M, Moeller A, Paululat A, Kümmel D. 2025. Mechanistic adaptation of the metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned. Science Advances. 11(35), eadx2893. View
Kettel P, Marosits L, Spinetti E, Rechberger M, Giannini C, Radler P, Niedermoser I, Fischer I, Versteeg GA, Loose M, Covino R, Karagöz GE. 2024. Disordered regions in the IRE1α ER lumenal domain mediate its stress-induced clustering. EMBO Journal. 43(20), 4668–4698. View
Vanhille-Campos CE, Whitley KD, Radler P, Loose M, Holden S, Šarić A. 2024. Self-organization of mortal filaments and its role in bacterial division ring formation. Nature Physics. 20, 1670–1678. View
Gnyliukh N, Johnson AJ, Nagel M, Monzer A, Babic D, Hlavata A, Alotaibi S, Isono E, Loose M, Friml J. 2024. Role of dynamin-related proteins 2 and SH3P2 in clathrin-mediated endocytosis in Arabidopsis thaliana. Journal of Cell Science. 137(8), jcs. 261720. View
Nußbaum P, Kureisaite-Ciziene D, Bellini D, Van Der Does C, Kojic M, Taib N, Yeates A, Tourte M, Gribaldo S, Loose M, Löwe J, Albers SV. 2024. Proteins containing photosynthetic reaction centre domains modulate FtsZ-based archaeal cell division. Nature Microbiology. 9(3), 698–711. View
ReX-Link: Martin Loose
Career
Since 2021 Professor, Institute of Science and Technology Austria (ISTA)
2015 – 2021 Assistant Professor, Institute of Science and Technology Austria (ISTA)
2011 – 2014 Departmental Fellow, Harvard Medical School, Boston, USA
2010 – 2011 Postdoc, TU Dresden and Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
2010 PhD, TU Dresden and Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
Selected Distinctions
2022 ERC Consolidator Grant
2016 HFSP Young Investigator Grant
2015 ERC Starting Grant
2012 – 2014 HSFP Long-term fellowship
2011 – 2012 EMBO Long-term fellowship
2010 Dr. Walter Seipp Award for best dissertation at TU Dresden
2001 – 2009 Student and PhD Fellowship of the German National Scholarship Foundation
