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Historical Background
Maintaining the integrity of the proteome is a tedious task. Nascent, misfolded, or denatured polypeptides are captured by molecular chaperones which try to fold them into their native conformations. Upon failure these polypeptides are channeled for degradation in a ubiquitin dependent manner, suggesting the presence of a link between chaperones and the 26S proteasome. An important feature of many chaperone-interacting proteins is the presence of tetratricopeptide repeats (TPR) which are protein-protein interacting motifs. In an attempt to identify novel TPR containing proteins, a cDNA fragment corresponding to nucleotides 721–1150 of CyP-40 (cytochrome P-40) was radiolabeled with [α-32P]dCTP and used to screen a phage library of human heart cDNA. Carboxy terminus of HSP70 Interacting Protein (CHIP) was identified through this screen. The gene for CHIP encodes for a 34.5 kDa protein which is well-conserved with an amino acid sequence similarity of...
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Acknowledgments
Financially supported by grants from CSIR, India (EMPOWER-OLP-002, MEDCHEM-BSC0108 & CSIR-MAYO: MLP-0017) and DST Nano Mission programme (SR/NM/NS-1058/2015) to Dr. Mrinal K Ghosh.
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Paul, I., Basu, M., Ghosh, M.K. (2018). CHIP. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101582
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DOI: https://doi.org/10.1007/978-3-319-67199-4_101582
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