Pattarawut Sopha, Ph.D.

Email: pattarawut@cgi.ac.th

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

Phone: (66)2 554 1900 ext 2643

Education

  • 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.

Publications: