![]() It is thought that a third of all proteins traffic through the endoplasmic reticulum (ER) for post-translational modifications (PTMs), folding, and trafficking ( Huh et al., 2003). Finally, these effects are examined in the context of lung structure, function, and disease.Įndoplasmic Reticulum Stress and the Unfolded Protein ResponseĬells are normally in a state of proteostasis, whereby networks of signaling pathways work in concert to maintain the proper synthesis, folding, trafficking, and degradation of proteins. This review also examines the overlooked role of post-translational modifications and their roles in protein processing and effects on ER stress and the UPR. When ER stress is excessive or prolonged and these mechanisms fail to restore proteostasis, the UPR triggers the cell to undergo apoptosis. The accumulation of unfolded/misfolded proteins in the endoplasmic reticulum (ER) causes ER stress and induces the unfolded protein response (UPR) and other mechanisms to restore ER homeostasis, including translational shutdown, increased targeting of mRNAs for degradation by the IRE1-dependent decay pathway, selective translation of proteins that contribute to the protein folding capacity of the ER, and activation of the ER-associated degradation machinery. 2McGill University, Montreal, QC, Canada.1Meakins-Christie Laboratories, Research Institute of the McGill University Health Centre (RI-MUHC), McGill University, Montreal, QC, Canada.Nakada 1,2 Rui Sun 1,2 Utako Fujii 1,2 James G. This chapter will describe our current understanding of SERCA structure, function, and regulation.Ĭalcium ATPase Phospholamban Sarcolipin Sarcoplasmic reticulum.Emily M. ![]() Second, an array of micropeptides concealed within long non-coding RNAs have been identified as new SERCA regulators. First, structures of the SERCA-SLN and SERCA-PLN complexes revealed molecular details of their interactions. The last few years have seen a renaissance in our understanding of SERCA regulatory subunits. Na +, K +-ATPase) has at least nine small transmembrane peptides that provide tissue specific regulation. Nonetheless, SERCA appeared to have only two regulatory subunits, while the related sodium pump (a.k.a. While our understanding of these regulatory mechanisms are still developing, SERCA and PLN are one of the best understood examples of peptide-transporter regulatory interactions. These two regulatory subunits play critical roles in cardiac contractility. PLN is expressed in cardiac muscle, whereas SLN predominates in skeletal and atrial muscle. Historically, SERCA is also known to be regulated by small transmembrane peptides, phospholamban (PLN) and sarcolipin (SLN). X-ray crystallographic studies have provided an extensive understanding of the intermediate states that SERCA populates as it progresses through the calcium transport cycle. In muscle cells, SERCA promotes relaxation by pumping calcium ions from the cytosol into the lumen of the sarcoplasmic reticulum (SR), the main storage compartment for intracellular calcium. ![]() synaptic transmission, muscle contraction, fertilization). As a calcium transporter, SERCA maintains the low cytosolic calcium level that enables a vast array of signaling pathways and physiological processes (e.g. Ca 2+-ATPase or SERCA) is a membrane transport protein ubiquitously found in the endoplasmic reticulum (ER) of all eukaryotic cells.
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