Christian Schlieker, PhD
Research & Publications
Biography
News
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.
Specialized Terms: DYT1 Dystonia, Membrane dynamics; Torsin ATPases; Alternative nuclear transport (nuclear egress); Protein quality control; viral pathogenesis
Coauthors
Research Interests
Biochemistry; Biophysics; Cell Biology; Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Selected Publications
- Dynamic quality control machinery that operates across compartmental borders mediates the degradation of mammalian nuclear membrane proteinsTsai P, Cameron C, Forni M, Wasko R, Naughton B, Horsley V, Gerstein M, Schlieker C. Dynamic quality control machinery that operates across compartmental borders mediates the degradation of mammalian nuclear membrane proteins. Cell Reports 2022, 41: 111675. PMID: 36417855, PMCID: PMC9827541, DOI: 10.1016/j.celrep.2022.111675.
- Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activitiesProphet SM, Rampello AJ, Niescier RF, Gentile JE, Mallik S, Koleske AJ, Schlieker C. Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities. Nature Cell Biology 2022, 24: 1630-1641. PMID: 36302970, PMCID: PMC10041656, DOI: 10.1038/s41556-022-01001-y.
- Nodal modulator (NOMO) is required to sustain endoplasmic reticulum morphologyAmaya C, Cameron C, Devarkar SC, Seager S, Gerstein MB, Xiong Y, Schlieker C. Nodal modulator (NOMO) is required to sustain endoplasmic reticulum morphology. Journal Of Biological Chemistry 2021, 297: 100937. PMID: 34224731, PMCID: PMC8327139, DOI: 10.1016/j.jbc.2021.100937.
- Lipid and protein dynamics that shape nuclear envelope identityBahmanyar S, Schlieker C. Lipid and protein dynamics that shape nuclear envelope identity. Molecular Biology Of The Cell 2020, 31: 1315-1323. PMID: 32530796, PMCID: PMC7353140, DOI: 10.1091/mbc.e18-10-0636.
- Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2Rampello AJ, Laudermilch E, Vishnoi N, Prophet SM, Shao L, Zhao C, Lusk CP, Schlieker C. Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2. Journal Of Cell Biology 2020, 219: e201910185. PMID: 32342107, PMCID: PMC7265317, DOI: 10.1083/jcb.201910185.
- The Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against DiseaseRampello AJ, Prophet SM, Schlieker C. The Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease. Biomolecules 2020, 10: 468. PMID: 32204310, PMCID: PMC7175109, DOI: 10.3390/biom10030468.
- Methodologies to monitor protein turnover at the inner nuclear membraneTsai PL, Zhao C, Schlieker C. Methodologies to monitor protein turnover at the inner nuclear membrane. 2019, 619: 47-69. PMID: 30910029, PMCID: PMC6457266, DOI: 10.1016/bs.mie.2018.12.033.
- Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1: a novel mode of regulation for AAA+ ATPasesChase A, Laudermilch E, Wang J, Shigematsu H, Yokoyama T, Schlieker C. Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1: a novel mode of regulation for AAA+ ATPases. The FASEB Journal 2018, 32: 114.1-114.1. DOI: 10.1096/fasebj.2018.32.1_supplement.114.1.
- Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1Chase AR, Laudermilch E, Wang J, Shigematsu H, Yokoyama T, Schlieker C. Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1. Molecular Biology Of The Cell 2017, 28: 2765-2772. PMID: 28814508, PMCID: PMC5638581, DOI: 10.1091/mbc.e17-05-0281.
- Dissecting Torsin/cofactor function at the nuclear envelope: a genetic studyLaudermilch E, Tsai PL, Graham M, Turner E, Zhao C, Schlieker C. Dissecting Torsin/cofactor function at the nuclear envelope: a genetic study. Molecular Biology Of The Cell 2016, 27: 3964-3971. PMID: 27798237, PMCID: PMC5156537, DOI: 10.1091/mbc.e16-07-0511.
- The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutationsTsai PL, Zhao C, Turner E, Schlieker C. The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations. ELife 2016, 5: e16011. PMID: 27336722, PMCID: PMC4951196, DOI: 10.7554/elife.16011.