title: Unfolding the complexities of ER chaperones in health and disease: report on the 11th international calreticulin workshop.
abstract: 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 2 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 Ca(2) regulation acting through its action in stress-related diseases, and the trafficking of glycoproteins to the cell surface. Central to maintaining healthy cell physiology is the correct ER-associated protein degradation of specific misfolded proteins. 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. These insights included the unfolded protein response, innate/adaptive immunity, tissue repair, the functions of calreticulin/chaperones from the cell surface, and extracellular environment. Diseases included 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.
authors.affiliation: Department of Medicine, New York University, 462 First Ave, New York, NY, 10016, USA. Leslie.Gold@nyumc.org.
authors.forename: Leslie
authors.initials: L
authors.lastname: Gold
authors.affiliation: Department of Biochemistry, University of Toronto, Toronto, ON, M5S 1A8, Canada.
authors.forename: David
authors.initials: D
authors.lastname: Williams
authors.affiliation: Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada.
authors.forename: Jody
authors.initials: J
authors.lastname: Groenendyk
authors.affiliation: Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada.
authors.forename: Marek
authors.initials: M
authors.lastname: Michalak
authors.affiliation: Institute of Biomedical and Clinical Science, University of Exeter School of Medicine, Devon, EX1 2LU, UK.
authors.forename: Paul
authors.initials: P
authors.lastname: Eggleton
mesh_terms: D000818:Animals; D037282:Calreticulin / Q000235:genetics / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D021381:Protein Transport; D056811:Unfolded Protein Response / Q000502:physiology*
chemical_list: C576483:CALR protein, human; D037282:Calreticulin; D018832:Molecular Chaperones
keywords: Calreticulin; Cancer modulation; ER associated protein degradation; ER stress; Glycoprotein folding; Immune regulation; Unfolded protein response; Wound healing