Christian Schlieker PhD

Assistant Professor of Molecular Biophysics and Biochemistry

Research Interests

DYT1 Dystonia, Membrane dynamics, Torsin ATPases, Alternative nuclear transport (nuclear egress), Protein quality control, viral pathogenesis


Research Summary

Mechanisms of membrane dynamics in relation to nuclear envelopathies and viral infection

Nuclear envelopathies are a diverse group of congenital diseases that are caused by mutations affecting proteins in the nuclear envelope or lamina. We hypothesize that envelopathy-associated alleles act at least in part through a gain of function mechanism that leads to a poisoning of nuclear membrane dynamics. Our goal is to unravel the cellular mechanisms that regulate protein homeostasis in the nuclear periphery, and to elucidate the role that these pathways play in muscular dystrophies, premature aging and related envelopathies. We exploit viral proteins known to manipulate the nuclear envelope as a novel approach to identify cellular factors involved in protein turnover and non-canonical nuclear transport via vesicular intermediates.


Selected Publications

  • Brown R, Zhao C, Chase A, Wang J, Schlieker C. The mechanism of Torsin ATPase activation. PNAS, in press.
  • Rose AE, Zhao C, Turner EM, Steyer AM, Schlieker C. Arresting a Torsin ATPase reshapes the endoplasmic reticulum. J Biol Chem. 2014 Jan 3;289(1):552-64. doi: 10.1074/jbc.M113.515791. Epub 2013 Nov 25.
  • Chenguang Zhao, Rebecca S. H. Brown, Anna R. Chase, Markus R. Eisele, and Christian Schlieker. Regulation of Torsin ATPases by LAP1 and LULL1 PNAS 2013. doi:10.1073/pnas.1300676110
  • Rose A, Schlieker C. Alternative nuclear transport for cellular protein quality control. Trends Cell Biol. 2012. Epub 2012/08/04. doi: 10.1016/j.tcb.2012.07.003.
  • Ernst R, Mueller B, Ploegh HL, Schlieker C. The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Molecular cell. 2009;36(1):28-38.

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