James Douglas Jamieson MD, PhD

Professor of Cell Biology; Special Advisor, MD/PhD Program

Research Interests

Endocrine pancreas; Secretory pathways; Lung development

Research Summary

For most of my research career, I have focused on the processes of synthesis, trafficking and exocytosis of secretory proteins from the pancreatic acinar cell which has served as the paradigm for examining the “Intracellular Aspects of the Process of Protein Secretion”*. My early work as a graduate student with George Palade at the Rockefeller University was involved in defining the role of the Golgi complex in the process which culminates in the formation of zymogen granules. Subsequently, among other topics, my laboratory examined the development and regulation of exocytosis of secretory proteins from the acinar cell, membrane biogenesis and polarity in epithelial cells, and the relationship of cell polarity to the basement membrane. Later work on this topic examined in detail the role of low Mr GTPases in regulated exocytosis. Since regulated exocytosis is accompanied by compensatory endocytosis of excess membrane inserted into the apical plasmalemma, we went on to illustrate an essential role of the actin cytoskeleton in this process and have demonstrated that proteins required for formation of endocytic vesicles (clathrin, adaptors, dynamin etc.) assemble at sites of exocytosis prior to compensatory membrane retrieval. After more than 30 years carrying out cell biologic research with an impressive and accomplished group of graduate students and postdoctoral fellows, I decided to close my laboratory in 2001 in order to focus my interests on teaching Cell Biology and Histology to first-year medical students. As part of my teaching interest, I also direct the MD/PhD Program at Yale University School of Medicine. This allows me to be involved in the education of both medical students and graduate students. The dual degree Program is meant to provide trainees with a broad exposure to human biology and medicine, and to an in-depth and rigorous training in one of the scholarly disciplines relevant to medicine. The ultimate goal of educating this group of students is to bridge the gap between basic research and clinical medicine.

Selected Publications

  • Van Weeren L, de Graff AM, Jamieson JD, Batenburg JJ, and Valentijn JA. (2004) Rab 3D and actin reveal distinct lamellar body subpopulations in alveolar epithelial cells. Am J Respir Cell Mol Biol. 30:288-295
  • Jena BP, Gumkowski F, Fischer von Mollard G, Jahn R, Jamieson JD. (1994) Redistribution of a rab-3 like GTP binding protein from secretory granules to the Golgi complex in pancreatic acinar cells during regulated exocytosis. J Cell Biol. 124: 43-53.
  • Valentijn JA, Valentijn K, Pastore LM, and Jamieson JD. (2000) Actin coating of secretory granules during regulated exocytosis correlates with the release of rab3D. Proc. Natl. Acad. Sci. USA. 97:1091-1095
  • Caplan MJ, Forbush B III, Palade GE, Jamieson JD. (1990) Biosynthesis of the Na,K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery. J Biol Chem. 265: 3528-3534.
  • Gorelick FS, Chang A, and Jamieson JD. (1987) Calcium-calmodulin-stimulated protein kinase in developing pancreas. Am. J. Physiol. 253:G469-G476
  • Jamieson, J.D. 2008. A tribute to George E. Palade. J.Clin.Invest. 118:3517-3518.
  • Riedel, D., W. Antonin, R. Fernandez-Chacon, G. Alvarez de Toledo, T. Jo, M. Geppert, J.A. Valentijn, K. Valentijn, J.D. Jamieson, T.C. Sudhof, and R. Jahn. 2002. Rab3D is not required for exocrine exocytosis but for maintenance of normally sized secretory granules. Mol.Cell.Biol. 22:6487-6497.
  • Qiu, X., J.A. Valentijn, and J.D. Jamieson. 2001. Carboxyl-methylation of Rab3D in the rat pancreatic acinar tumor cell line AR42J. Biochem.Biophys.Res.Commun. 285:708-714.
  • Jamieson, J. D. and S. M. Friedman. 1961. Sodium and potassium shifts associated with peripheral resistance changes in the dog. Circ. Res. 9:996-1004.
  • Jamieson, J. D. and G. E. Palade. 1964. Specific granules in atrial muscle cells. J. Cell Biol. 23:151-172.


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