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Hsp70 Chaperone Systems in Vesicular Trafficking

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Cellular Trafficking of Cell Stress Proteins in Health and Disease

Part of the book series: Heat Shock Proteins ((HESP,volume 6))

Abstract

In humans there are 13 different Hsp70 proteins and 50 J proteins (also known as DnaJ or Hsp40 proteins; Kampinga et al., Cell Stress Chaperones 14:105–111, 2009). This diversity of the cochaperone J protein allows the recruitment of Hsp70 family members to multiple cellular locales and activities beyond their canonical protein folding functions (Cheetham and Caplan AJ, Cell Stress Chaperones 3:28–36, 1998; Kampinga and Craig, Nat Rev Mol Cell Biol 11:579–592, 2010). Significant amongst these roles is the participation of Hsp70 systems in intracellular traffic of membranes, including involvement in regulation of endocytosis and exocytosis mechanisms. In this chapter we describe the core components of Hsp70 chaperone systems and consider their multiple functions, from the perspective of J proteins acting as targeting factors for Hsp70 activity. We then focus on the role of Hsp70 chaperone systems in intracellular trafficking of vesicles and the fate of vesicular trafficked proteins.

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Chapple, J.P., Parfitt, D., Campbell, D. (2012). Hsp70 Chaperone Systems in Vesicular Trafficking. In: Henderson, B., Pockley, A. (eds) Cellular Trafficking of Cell Stress Proteins in Health and Disease. Heat Shock Proteins, vol 6. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-4740-1_6

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