Unfolding the complexities of ER chaperones in health and disease: Report on the 11th International Calreticulin Workshop
Cell Stress and Chaperones
Springer Verlag (Germany)
© Cell Stress Society International 2015
Reason for embargo
The 11th International Calreticulin workshop was held May 15–18, 2015 at New York University School of Medicine-Langone Medical Center, New York. The meeting highlighted many of the new discoveries in the past two years involving the important role of molecular chaperones in physiological and pathological processes. Crucial to the understanding of these disease processes was the role of chaperones in maintaining quality control of protein processing in the endoplasmic reticulum, the importance of Ca2regulation acting through its action in stress-related diseases, and the trafficking of glycoproteins to the cell surface. Central to maintaining healthy cell physiology involves correct ER-associated protein degradation of specific misfolded proteins and information on different mechanisms involved in the degradation of misfolded proteins was revealed. This was a landmark meeting for the chaperone field in terms of new insights into their roles in physiology including the unfolded protein response, innate/adaptive immunity, tissue repair, the functions of calreticulin/chaperones from the cell surface and extracellular environment and in diseases including from neurodegenerative disorders, prion disease, autoimmunity, fibrosis-related disease, the host immune response to cancer and hematologic diseases associated with calreticulin mutations. . The 12th calreticulin workshop is planned for the spring of 2017 in Delphi, Greece.
The final publication is available at Springer via http://dx.doi.org/10.1007/s12192-015-0638-4
Cell Stress and Chaperones, 2015, Volume 20, Issue 6, pp.875-883