Precise folding of nascent proteins is central to a diverse spectrum of biological functions. To avoid the perils of protein misfolding, cells harbor a complex network of molecular chaperones residing in the endoplasmic reticulum (ER) that promote efficient protein folding and ensure the maintenance of protein homeostasis (proteostasis). Even though long-term memory consolidation and persistent forms of synaptic plasticity require the activity-induced synthesis of new proteins in the hippocampus, the physiological relevance of the protein folding machineries in learning and memory remains poorly understood. Importantly, ongoing research supports the hypothesis that memory impairments pertinent to several neurodegenerative disorders share a common etiology - that they are likely mediated by the misfolding and aberrant aggregation of select proteins that disrupt the cellular proteostasis. My research aims at defining the role and the mechanistic underpinnings of the ER chaperones in driving long-term memory storage, as well as elucidate the implications of chaperone functioning in the context of neurodegeneration. A comprehensive understanding of such mechanisms will empower us to implement novel therapeutic interventions against cognitive deficits associated with neurogenerative disorders.