Research

Briefly:

Cells routinely sample their local environment, process this information through internal signaling, and respond accordingly. However, the sheer complexity that underlies cellular behavior makes cells notoriously difficult to understand and control. How can we reach a detailed understanding of complex biological systems? Traditionally, biologists have advanced knowledge by employing a top-down approach starting from a living organism, manipulating it and investigating its responses. This has generated a vast amount of information but has sometimes struggled to isolate the individual mechanisms that make up a complex process. To address these issues, traditional approaches are now being complemented with an engineering-inspired approach.  I work on the development of  ‘cell-like’ systems component-by-component from the bottom-up. Assembly of cellular building blocks should lead to the reproduction of cellular functions outside a living system, thereby constructing a highly simplified artificial cell. This approach is powerful in understanding how biological systems are built and will help us develop strategies for therapeutic intervention.

PUBLICATIONS

(* authors contributed equally)

Schmid EM*, Bakalar M*, Choudhuri K, Weichsel J, Ann HS, Geissler PL, Dustin ML, Fletcher DA. Size-dependent protein segregation at membrane interfaces. Nature Physics. Published online: 7 March 2016 | doi: 10.1038/nphys3678

Schmid EM, Richmond DL, Fletcher DA. Reconstitution of proteins on electroformed vesicles. Methods in Cell Biol. 2015; 128:319-38

Stachowiak JC *, Schmid EM*, Ryan C.J., Ann H.S., Sasaki D.Y., Sherman M.B. Geissler P.L., Fletcher D.A., Hayden C.C. (2012) Membrane bending by protein-protein crowding. Nat Cell Biol. 2012 Sep;14(9):944-9. doi: 10.1038/ncb2561. Epub 2012 Aug 19.

Highlighted in: T. Kirchhausen. “Bending membranes” Nat. Cell. Biol. 2012 Sep;14(9):906-8. doi: 10.1038/ncb2570.

HighMag Science blog: http://highmagblog.blogspot.com

Larochelle S. “Bent out of shape“. Nat Struct Mol Biol. 2012 Oct 4;19(10):982. doi: 10.1038/nsmb.2409.

Richmond DL*, Schmid EM*,Martens S, Stachowiak JC, Liska N, Fletcher DA (2011) Forming giant vesicles with controlled membrane composition, asymmetry, and contents. Proc Natl Acad Sci U S A. 2011 May 18 

In the news: Der Standard  and Oberösterreichische Nachrichten

Olesen LE*, Schmid EM*, Ford MG*, Vallis Y, Babu MM, Li P, Mills IG, Evans PR, McMahon HT*, Praefcke GJ* (2008) Solitary and repetitive binding motifs for the AP2 complex alpha-appendage in amphiphysin and other accessory proteins. J Biol Chem 283:5099–109.

Schmid EM, McMahon HT (2007) Integrating molecular and network biology to decode endocytosis. Nature 448:883–8.

Burtey A, Schmid EM*, Ford MG*, Rappoport JZ*, Scott MGH*, Marullo S, Simon SM, McMahon HT, Benmerah A. (2007) The conserved isoleucine-valine-phenylalanine motif couples activation state and endocytic functions of beta-arrestins. Traffic 8:914–31.

Schmid EM*, Ford MG*, Burtey A, Praefcke GJ, Peak-Chew SY, Mills IG, Benmerah A, McMahon HT (2006) Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly. PLoS Biol 4:e262.

Sousa C, Schmid EM, Skern T (2006) Defining residues involved in human rhinovirus 2A proteinase substrate recognition. FEBS Letters 580:5713–7.

Praefcke GJ*, Ford MG*, Schmid EM, Olesen LE, Gallop JL, Peak-Chew SY, Vallis Y, Babu MM, Mills IG, McMahon HT (2004) Evolving nature of the AP2 alpha-appendage hub during clathrin-coated vesicle endocytosis. EMBO J 23:4371–83.

Foeger N, Schmid EM, Skern T (2003) Human rhinovirus 2 2Apro recognition of eukaryotic initiation factor 4GI. Involvement of an exosite. J Biol Chem 278:33200–7.

PATENT

J. C. Stachowiak, T. H. Li, S. Parekh, A. P. Liu, D. L. Richmond, E.M. Schmid, D. A. Fletcher. “Forming an Artificial Cell with Controlled Membrane Composition, Asymmetry, and Contents,” US Provisional Patent Pending.

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