Executive Summary : | The endoplasmic reticulum (ER) is a crucial site for protein folding and maturation, and under stress conditions, unfolded and misfolded proteins accumulate in the ER, leading to the activation of the UPR response. This process is essential for normal cell physiology and ER stress adaptation. Under severe stress, the UPR triggers a signaling switch that favors cell death and apoptosis. ER-resident transmembrane proteins, such as PERK, ATF6, and IRE1, activate the UPR response by competing with GRP78 for binding. The study aims to understand the role of stress-induced endoplasmic reticulum membrane proteins in the UPR response for developing stress-resilient chickpea. The hypothesis is to determine the specific role of membrane protein in the stress response of chickpea and determine the kinetic response of the ER membrane during drought stresses. The function of the ER membrane will be tested through loss-of-function and selective overexpression, with the long-term goal of optimizing chickpea growth under suboptimal conditions. Several questions are raised, including whether the insertion of TMDs to cause UPR includes the membrane protein of ER, what chemical mechanisms can be used to reduce the stress response, if there are chaperone-like roles in plant ER, and what aspect of a substrate protein the ER membrane safeguards and supports biogenesis. Chickpea, the third-ranked food legume crop globally, faces significant constraints due to dehydration stress, resulting in approximately 40-50% yield loss. Understanding the role of ER membrane proteins in alleviating stress response is crucial for developing stress resilience crops and ensuring crop yield. |