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Editorial
, Volume: 18( 1)Molecular Chaperones: Guardians of Protein Folding and Cellular Homeostasis
Molecular chaperones are specialized proteins that assist other proteins in achieving and maintaining their correct three-dimensional structures, preventing misfolding and aggregation that can compromise cellular function. These proteins play a critical role in cellular homeostasis, particularly under conditions of stress such as heat shock, oxidative stress, and exposure to toxins. Key classes of molecular chaperones include heat shock proteins (HSPs), chaperonins, and small chaperones, each facilitating protein folding through distinct mechanisms. Beyond protein folding, chaperones are involved in protein trafficking, degradation, and the assembly of multiprotein complexes. Dysfunction of molecular chaperones has been linked to a variety of diseases, including neurodegenerative disorders, cancer, and metabolic syndromes. This article reviews the importance of molecular chaperones in maintaining protein quality control and their broader implications for cellular physiology and disease prevention. Keywords: Molecular chaperones, heat shock proteins, protein folding, protein homeostasis, chaperonins, cellular stress
Abstract
Proteins are the workhorses of the cell, executing diverse functions that range from enzymatic catalysis to structural support. However, proteins are highly susceptible to misfolding due to their complex three dimensional structures, environmental stress, or errors in synthesis. Molecular chaperones are a vital class of proteins that assist in the correct folding, stabilization, and maintenance of other proteins, ensuring proper cellular function. These chaperones do not provide structural information but instead facilitate the folding process by preventing inappropriate interactions and aggregation. Heat shock proteins (HSPs), among the most studied molecular chaperones, are upregulated in response to cellular stress and help restore proteostasis. Chaperonins, such as the GroEL/GroES complex in bacteria and the TRiC/CCT complex in eukaryotes, form cage-like structures that provide an isolated environment for proteins to fold correctly. Small chaperones, including HSP27 and αB-crystallin, act as holdases, binding partially folded proteins to prevent aggregation until they can achieve their native state. Beyond folding, molecular chaperones contribute to protein trafficking by guiding proteins to their proper cellular compartments, regulate the assembly of multiprotein complexes, and direct irreparably damaged proteins toward degradation pathways such as the ubiquitin-proteasome system. The significance of molecular chaperones becomes particularly evident under pathological conditions. Misfolded proteins are implicated in neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s disease, where chaperone Citation: Omar Farooq. Molecular Chaperones: Guardians of Protein Folding and Cellular Homeostasis. Biochem Ind J. 19(1):202. 1 © 2025 Trade Science Inc. www.tsijournals.com | December-2025 dysfunction exacerbates protein aggregation. In cancer, some chaperones are overexpressed to stabilize mutated oncogenic proteins, highlighting their dual role in physiology and pathology. Studying molecular chaperones offers valuable insight into cellular quality control mechanisms and presents potential therapeutic strategies to mitigate diseases associated with protein misfolding and aggregation. Conclusion Molecular chaperones are indispensable for maintaining protein homeostasis and ensuring cellular health. By facilitating proper protein folding, preventing aggregation, and participating in protein trafficking and degradation, they act as guardians of cellular integrity. Understanding their mechanisms and regulation not only deepens our knowledge of fundamental cell biology but also provides critical avenues for therapeutic intervention in diseases linked to protein misfolding and stress. The continued exploration of molecular chaperones promises to reveal novel insights into cellular resilience and adaptability.
