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 using a bottom-up synthetic biology approach.

Although most individual players required for specific cellular processes have been identified, how they act together to accomplish their specific 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 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 identify formation and vesicle transport?

Contact

Martin Loose
Institute of Science and Technology Austria (IST Austria)
Am Campus 1
A – 3400 Klosterneuburg
E-mail: martin.loose@remove-this.ist.ac.at

CV and Publication List

Martin Loose's website

Assistant
Rita Six

Phone: +43 (0)2243 9000-1165
E-mail: rita.six@remove-this.ist.ac.at

Team

  • Natalia Baranova, Postdoc
  • Urban Bezeljak, PhD Student
  • Paulo Dos Santos Caldas, PhD Student
  • Christian Düllberg, Postdoc
  • Katrin Loibl, Technician
  • Maria Lopez Pelegrin, Technician

Current Projects

  • Identifying biochemical networks that determine intracellular organization |
  • Studying the mechanism of bacterial cell division

 

Selected Publications

  • Loose M, Mitchison TJ. (2014) The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns, Nat Cell Biol 16, 38–46.
  • Bonny M, Fischer-Friedrich E, Loose M, Schwille P, Kruse K. (2013) Membrane Binding of MinE Allows for a Comprehensive Description of Min-Protein Pattern Formation, PLoS Comp Biol 9, e1003347.
  • Schweizer* J., Loose* M. et al. (2012) Geometry sensing by self-organized protein patterns, Proc. Natl. Acad. Sci. U.S.A. 109, 15283–15288. *equal contribution.
  • Loose M, Fischer-Friedrich E, Herold C, Kruse K, Schwille P. (2011) Min protein patterns emerge from rapid rebinding and membrane interaction of MinE, Nature Structural & Molecular Biology 18, 577–583.
  • Loose M, Kruse K, Schwille P. (2011) Protein Self-Organization: Lessons from the Min System, Annual Review of Biophysics 40, 315–336.
  • Dinarina A*, Pugieux C*, Mora Corral M, Loose M, et al. (2009) Chromatin shapes the mitotic spindle, Cell 138, 502–513. *equal contribution.
  • Loose M, Fischer-Friedrich E, Ries J, Kruse K, Schwille P. (2008) Spatial regulators for bacterial cell division self-organize into surface waves in vitro, Science 320, 789–792.

Career

Since 2015 Assistant Professor, IST Austria

2011-2014 Departmental fellow, Department of Systems Biology, Harvard Medical School, Boston, USA
2010-2011 Postdoc, TU Dresden and MPI-CBG, Dresden, Germany
2010 PhD, TU Dresden and MPI-CBG, Dresden, Germany

Selected Distinctions

2015 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 (‘Studienstiftung des deutschen Volkes’)