Table of Contents

A View of the Endoplasmic Reticulum Through the Calreticulin Lens.- Structural Analysis of Calreticulin, an Endoplasmic Reticulum-Resident Molecular Chaperone.- The Role of Endoplasmic Reticulum Chaperones in Protein Folding and Quality Control.- Proteins Interacting with STIM1 and Store-Operated Ca2+ Entry.- Endoplasmic Reticulum (ER) and ER-Phagy.- Defects in Protein Folding and/or Quality Control Cause Protein Aggregation in the Endoplasmic Reticulum.- Roles of Calreticulin in Protein Folding, Immunity, Calcium Signaling and Cell Transformation.- Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease.- Cancer Biology of the Endoplasmic Reticulum Lectin Chaperones Calreticulin, Calnexin and PDIA3/ERp57.- Maintenance of Endoplasmic Reticulum Protein Homeostasis in Cancer: Friend or Foe.- IP3 Receptor Biology and Endoplasmic Reticulum Calcium Dynamics in Cancer.- Disruption of Endoplasmic Reticulum Proteostasis in Age-Related Nervous System Disorders.- Endoplasmic Reticulum Homeostasis and Stress Responses in Caenorhabditis elegans.- Tardigrada: An Emerging Animal Model to Study the Endoplasmic Reticulum Stress Response to Environmental Extremes.

About the Author

Marek Michalak obtained his PhD degree in Biochemistry from the Nencki Institute for Experimental Biology (Poland). He is a Distinguished University Professor in the Department of Biochemistry at the University of Alberta (Canada). His research interests are in the areas of molecular chaperones, protein folding and regulation of calcium homeostasis. Agellon and Michalak have an ongoing research collaboration that has spanned two decades investigating the nature of the mechanisms involved in the integration and coordination of cellular processes and metabolism.

Luis Agellon received his PhD degree from McMaster University (Canada) and is currently a Professor in School of Human Nutrition at McGill University. His major research area is in nutrient control of gene expression and metabolism.