Huntingtin Yeast Two-Hybrid Protein K (HYPK): An Intrinsically Unstructured Heat Shock Inducible Protein with Diverse Ce
Huntingtin Yeast Two-Hybrid Protein K (HYPK) was identified as huntingtin interacting protein in yeast 2 hybrid (Y2H) assay in 1998. Since then, HYPK has been characterized and shown to participate in diverse cellular functions. HYPK is shown to possess c
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Abstract Introduction Huntingtin Yeast Two-Hybrid Protein K (HYPK) was identified as huntingtin interacting protein in yeast 2 hybrid (Y2H) assay in 1998. Since then, HYPK has been characterized and shown to participate in diverse cellular functions. HYPK is shown to possess chaperone like activity in vitro and in vivo and regulated by Heat Shock Factor 1 (HSF1) by binding to the promoter of HYPK in response to heat shock (HS). The goal of the present review is to describe and evaluate current information of HYPK. Methods We searched published literatures and various databases to get information of HYPK. Results Result is divided into two parts. In first part, we briefly describe regulation of genes coded for heat shock proteins (HSP) and noncoding RNAs by HSF1. Role of HSP in different biological processes/functions is also summarized. Next, we N. P. Bhattacharyya (*) Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, Kolkata, West Bengal, India e-mail: [email protected]; [email protected] S. Das Department of Biology, Aging Mind and Brain Initiative, 143 Biology Building, University of Iowa, Iowa City, IA, USA K. R. Choudhury Cell Biology & Physiology Division, CSIR-Indian Institute of Chemical Biology (TRUE), Kolkata, West Bengal, India S. Raychaudhuri CSIR-Centre for Cellular and Molecular Biology, Hyderabad, Telangana, India J. Ghose Department of Radiation Oncology, James Cancer Hospital and Richard Solove Research Institute, The Ohio State University, Columbus, OH, USA © Springer Nature Switzerland AG 2020 A. A. A. Asea, P. Kaur (eds.), Heat Shock Proteins in Neuroscience, Heat Shock Proteins 20, https://doi.org/10.1007/7515_2020_22
N. P. Bhattacharyya et al.
discuss biophysical, biological characteristics and regulation of HYPK in the light of regulation of genes coding for HSP. HYPK is an intrinsically unstructured protein with chaperone activity and regulated by HSF1 in response to HS. Like many HSP, HYPK suppresses heat shock response via an auto-regulatory loop, binds to nascent polypeptides and interacts with more than 70 proteins, including transcription factors HSF1, TP53, RELA/p65. Role of HYPK-TFs interaction in modulating target genes of TFs remains unknown. HYPK involves in cell proliferation, cell cycle regulation, apoptosis and autophagy. Conclusions Taken together, we conclude that HYPK is a heat shock protein with chaperone activity. Based on the result, activation of HYPK could be one of the approaches to reduce aggregates and toxicity in HD. Keywords Apoptosis · Autophagy · Cell cycle · Chaperone · Heat shock response · HYPK · Intrinsically unstructured protein · Nascent peptides
Abbreviations HS HSE HSF HSP HSR HTT HYPK IDP IUP lncRNA miRNA TF Y2H
heat shock heat shock element heat shock transcription factor heat shock proteins heat shock response huntingtin Huntingtin Yeast Two-Hybrid Protein K intrinsically disordered protein intrinsically unstructured protein long non-coding RNA microRNA transcription factors yeast two-hybrid
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