Protein trafficking describes the complex processes that ensures the accurate delivery of proteins to their target destinations within a cell. It involves a series of regulatory steps, including protein folding, assembly, transport, and localization. Chaperones play a crucial role in protein trafficking by assisting in these processes and ensuring the fidelity of protein folding and correct targeting. Additionally, chaperones also have important roles in cell signalling, where they can regulate protein-protein interactions and thereby contribute to signal transduction pathways. Chaperones facilitate proper protein folding by preventing misfolding, aggregation, or inappropriate degradation of proteins. They bind to nascent or misfolded proteins, providing them with a protected environment for correct folding to occur. Notable chaperone families involved in this process include heat shock proteins (HSPs), such as Hsp70 and Hsp90. Chaperones also participate in protein quality control by identifying misfolded or damaged proteins and directing them for refolding or degradation. This process ensures the maintenance of cellular homeostasis and prevents the accumulation of toxic protein aggregates. The chaperone-associated ubiquitin ligase CHIP (carboxyl terminus of Hsp70-interacting protein) is an example of a chaperone that mediates the degradation of misfolded proteins via the ubiquitin-proteasome system. Chaperones also aid in the assembly of multiprotein complexes by coordinating the interactions between their constituent subunits. They thereby ensure the correct stoichiometry and structural integrity of these complexes. For instance, the chaperone CCT (chaperonin-containing TCP-1) assists in the folding and assembly of tubulin, which is essential for microtubule formation. Chaperones are also involved in regulating some protein-protein interactions involved in cell signalling pathways. They can either promote or inhibit specific interactions, thus modulating signalling cascades. One example is the Hsp90 chaperone, which stabilizes and activates client proteins, including various kinases and steroid hormone receptors. Chaperones also influence the activity and localization of transcription factors, which are crucial regulators of gene expression. They can assist in the folding and maturation of transcription factors, ensuring their proper function. For example, the chaperone Hsp70 plays a role in the activation of the heat shock transcription factor HSF1. Chaperones are also known to contribute to the assembly of multi-protein complexes known as signalosomes, which serve as platforms for signal transduction. Here they often act as scaffolds, facilitating the recruitment and organization of multiple signalling molecules into functional complexes. The chaperone Hsp90 for example is involved in the assembly of numerous signalosomes, such as the mTORC1 (mechanistic target of rapamycin complex 1). Finally, chaperones are important components of cellular stress response pathways, protecting cells from various stresses. Here they assist in refolding damaged proteins and promote cell survival under stressful conditions. For example, one of the small heat shock proteins Hsp27 plays a role in protecting cells from oxidative stress. Thus, chaperones play indispensable roles in protein trafficking and cell signalling. They ensure proper protein folding, assembly, and transport, contributing to the maintenance of cellular homeostasis. Additionally, chaperones participate in cell signalling by modulating protein-protein interactions, regulating transcription factors, and organizing signalosomes. We offer a comprehensive product range of research tools for investigating chaperones, including Hsp27 antibodies, Albumin antibodies, Hsp60 antibodies, Hsp27 ELISA Kits, and Hsp70 ELISA Kits. Explore our full chaperones product range below and discover more, for less. Alternatively, you can explore our Heat Shock Proteins product range.