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Loose Group

Self-Organization of Protein Systems

How are nanometer-sized proteins able to perform complex functions on a cellular scale? The Loose group studies the molecular mechanisms of intracellular self-organization by rebuilding cellular functions in a bottom-up approach.


Although we often know which proteins are required for specific processes in the cell, how they act together to accomplish this task is not yet understood. Instead of looking at complex phenomena in an intact cell, the Loose group aims to rebuild cellular functions from purified components. This bottom-up approach allows for a better control of the experimental conditions and a quantitative characterization of the underlying molecular processes. Ultimately, this helps to identify the mechanistic principles that allow to give rise to living systems. The interdisciplinary approach of the Loose group combines biochemical reconstitution experiments with advanced fluorescence microscopy, biomimetic membrane systems, and computer-aided image analysis. They currently focus on two research questions: (1) What is the mechanism of bacterial cell division?, and (2) What are the emergent properties of small GTPase networks involved in membrane identity formation and vesicle transport?




Team

Image of Albert Auer

Albert Auer

PhD Student

Image of Anita Carija

Anita Carija

Research Technician

Image of Caterina Giannini

Caterina Giannini

PhD Student


Image of Roman Hajdu

Roman Hajdu

PhD Student

Image of Himani Khurana

Himani Khurana

Postdoc

Image of Marko Kojic

Marko Kojic

PhD Student


Image of Olesia Ledovich

Olesia Ledovich

Research Technician

Image of Ivana Matijevic

Ivana Matijevic

PhD Student

Image of Arsenii Solovev

Arsenii Solovev

PhD Student


Image of Benjamin Springstein

Benjamin Springstein

Postdoc

Image of Xing Ye

Xing Ye

Postdoc


Current Projects

Self-organization of the bacterial cell division machinery | Emergent properties of small GTPase networks


Publications

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. 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. 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., 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

Radler P, Loose M. 2024. A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches. European Journal of Cell Biology. 103(1), 151380. View

View All Publications

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


Additional Information

Open Loose group website



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