Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi


  • Indranil Paul
  • Malini Basu
  • Mrinal K. GhoshEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101582



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 H SP70 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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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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Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Proteomics Program, Novo Nordisk Foundation Center for Protein ResearchUniversity of CopenhagenCopenhagenDenmark
  2. 2.Department of MicrobiologyBarrackpore Rastraguru Surendranath CollegeBarrackpore, KolkataIndia
  3. 3.Cancer Biology and Inflammatory Disorder DivisionCouncil of Scientific and Industrial Research-Indian Institute of Chemical Biology (CSIR-IICB)KolkataIndia