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Moonlighting Functions of Heat Shock Protein 90

  • Chang Chen
  • Constance JefferyEmail author
Chapter
Part of the Heat Shock Proteins book series (HESP, volume 19)

Abstract

Hsp90 is a highly expressed and ubiquitous chaperone in eukaryotes and bacteria. It works with hundreds of client proteins and is regulated by dozens of co-chaperones. Its functions in folding, stabilizing, assembling and disassembling proteins and complexes that are involved in many key processes in the cell, including antigen cross-presentation, stabilization of the cytoskeleton, signaling pathways, stabilization of steroid receptors and other transcription factors, assembly and disassembly of transcription machinery, DNA repair, and the cell cycle. This ubiquitous and versatile intracellular protein is found to have even more functions outside the cell. In this review we discuss the idea that Hsp90 is a moonlighting protein with roles as a secreted cytokine and as a cell surface apoptotic signal and receptor for bacterial cells and lipopolysaccharide.

Keywords

Chaperone Cytokine HSP90 Moonlighting protein Receptor Secretion 

Abbreviations

A2MR

Alpha 2 macroglobulin receptor

BMDC

Bone marrow derived dendritic cells

CD11

Integrin subunit

CD18

Integrin subunit

CXCR4

Chemokine receptor 4

ER

Endoplasmic reticulum

GDF5

Growth differentiation factor 5

HEp-2

Human epithelial type 2

Hsc70

Heat shock cognate 71 kDa protein

hsp75

Heat shock protein 75 kDa mitochondrial

Hsp90

Heat shock protein Hsp 90

HtpG

High temperature protein G/C62.5

LBP

Lipopolysaccharide-binding protein

LOX-1

Lectin-like oxidized LDL receptor-1

LPS

Lipopolysaccharide

LRP-1

LDL receptor-related protein 1/ CD91

MoonProt

Moonlighting proteins database

PTMs

Post-translational modifications

TLR4

Toll-like receptor 4

TRAP1

Heat shock protein 75 kDa mitochondrial

Notes

Acknowledgements

Research on this project in the Jeffery lab is supported by an award from the University of Illinois Cancer Center.

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Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  1. 1.Department of BioengineeringUniversity of Illinois at ChicagoChicagoUSA
  2. 2.Department of Biological SciencesUniversity of Illinois at ChicagoChicagoUSA

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