PROTEOMIC LANDSCAPE OF STRESS-INDUCED CELLULAR REPROGRAMMING

Abstract

Environmental stress situations such as changes in temperature, salinity, drought conditions and pollution coupled with biotic stressors such as pathogens and interactions among microbes severely interfere with the cellular homeostasis and biological activities. In order to survive in these dynamic conditions, cells are reprogrammed upon stress conditions, allowing them to quickly adapt in a coordinated manner, through concerted molecular responses. Although earlier research has widely utilized genomic and transcriptomic changes, these techniques cannot aid in capturing the functional implications of changes in proteins.

It is here that proteomics has become an effective methodology to study the dynamic nature of stress-induced changes in protein expression, modification, and interaction. Complex intracellular signaling pathways, such as reactive oxygen species (ROS) signaling and mitogen-activated protein kinase (MAPK) cascades are triggered by stress signals and eventually coordinate protein synthesis, folding, and degradation. The results of these processes comprise large scale changes in the proteome such as stress-responsive protein induction, post-translational modifications and reorganization of protein networks.

The described proteomic adaptations are vital to the cellular resilience, therefore, the ability to make metabolic changes and the survival in the long-term. Moreover, proteomic modifications can also contribute to the adaptive memory processes, wherein cells have a better response to repeat stress events. Knowledge of the proteomic profile of stress-induced cell reprogramming sheds further light on the functional cellular responses, as well as presents potential applications in biomedical studies, agriculture, and biotechnology.