Pattarawut Sopha, Ph.D.


Office: Chulabhorn Graduate Institute Building, 6th Floor, Room Faculty Office 2

Phone: (66)2 554 1900 ext 2643


  • 2013-2016 Postdoctoral, The University of North Carolina - Chapel Hill
  • 2008-2012 Ph.D. (Biological Sciences) Nara Institute of Science and Technology
  • 2002-2005 M.Sc. (Molecular Genetics and Genetic Engineering) Mahidol University
  • 1998-2002 B. Sc. (Microbiology) Srinakharinwirot University

Research Interests:

Protein homeostasis is an essential cellular adaptation. Improper balance between protein production, folding, and degradation can lead to proteotoxicity, and subsequently cell death (apoptosis). In humans, protein folding defect, immature protein degradation, and unfavorable protein aggregation are considered to be causes of diseases such as neurodegeneration and lung fibrosis. Eukaryotic cells are composed of subcellular compartments that have specific tasks in maintaining cell viability. Among them, the endoplasmic reticulum (ER), in mammalian cells, produces about one-third of total cellular proteins, including soluble and transmembrane proteins, and also provides protein modifications to secretory proteins. Disturbance of the ER generates a situation called ER stress causing an accumulation of misfolded or unfolded proteins. To maintain protein homeostasis, the ER is protected by intracellular stress signaling pathways that transcriptionally control the availability of protein folding machineries or ER chaperones. In addition, excessive unfolded or misfolded proteins can be eliminated by ER-associated protein degradation (ERAD), in which the target proteins are retrotranslocated from the ER and then degraded by cytosolic proteasomes via assistance of chaperones or protein quality control factors.

My research focuses on the investigation of protein homeostasis in mammalian cells. I am particularly interested in studying how chaperones and protein quality control (PQC) factors are regulated and function under proteotoxic stress induced by pathophysiological conditions, chemicals, and environmental factors. Specifically, the condition that cells are disturbed by proteotoxicity from accumulation and aggregation of unfolded or misfolded proteins. I use techniques in Biochemistry (such as cell fractionation, protein purification, and metabolic labeling) and Molecular Biology (for example gene cloning, heterologous gene expression) to answer basic science questions and phenomena in a field of Cell Biology.

Selected Publications:

The ER-transmembrane Hsp40 DNAJB12 is sensitive to acute ER stress and degraded beforein response to ER stress- induced apoptosis. Sopha P, Ren HY, Cyr DM (Manuscript in prep.)

Restoration of R117H CFTR Folding and Function in Human Airway Cells Through Combination Treatment with VX-809 and VX-770. Gentzsch M, Ren HY, Houck SA, Quinney NL, Cholon DM, Sopha P, Chaudhry IG, Das J, Dokholyan NV, Randell AH, Cyr DM. Am J Physiol Lung Cell Mol Physiol. 311 L550–L559 (2016 September)

VX-809 corrects folding defects in cystic fibrosis transmembrane conductance regulatorprotein through action on membrane-spanning domain 1. Ren HY, Grove DE, De La Rosa O, Houck SA, Sopha P, Goor FV, Hoffman BJ, Cyr DM Mol Biol Cell. 24 p3016-24 (2013 August)

A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins. Sopha P, Kadokura H, Yamamoto Y, Takeuchi M, Saito M, Tsuru A, Kohno K. Cell Struct. Funct. 37 p177-187 (2012 September)

Domain compatibility in Ire1 kinase is critical for the unfolded protein response. Poothong J, Sopha P, Kaufman RJ, Tirasophon W. FEBS Lett. 584 p3203 – 3208 (2010 June)

Full list of publications