Neurochemical Research

, Volume 42, Issue 2, pp 406–414 | Cite as

Targeting of Heat Shock Protein HSPA6 (HSP70B′) to the Periphery of Nuclear Speckles is Disrupted by a Transcription Inhibitor Following Thermal Stress in Human Neuronal Cells

Original Paper

Abstract

Heat shock proteins (Hsps) are a set of highly conserved proteins involved in cellular repair and protective mechanisms. The intracellular localization of inducible members of the HSPA (HSP70) family can be used as an index to identify stress-sensitive sites in differentiated human neuronal cells. Following thermal stress, the little studied HSPA6 (HSP70B′) was targeted to the periphery of nuclear speckles (perispeckles) that are sites of transcription factories. Triptolide, a fast-acting transcription inhibitor, knocked down levels of the large subunit of RNA polymerase II, RPB1, during the time-frame when HSPA6 associated with perispeckles. Administration of triptolide to heat shocked human neuronal SH-SY5Y cells, disrupted HSPA6 localization to perispeckles, suggesting the involvement of HSPA6 in transcriptional recovery after stress. The HSPA6 gene is present in the human genome but is not found in the genomes of the mouse and rat. Hence current animal models of neurodegenerative diseases lack a member of the HSPA family that exhibits the feature of stress-induced targeting to perispeckles.

Keywords

HSPA6 (HSP70B′) Human neuronal SH-SY5Y cells Triptolide 

Notes

Acknowledgments

This research is supported by grants from Natural Sciences and Engineering Research Council (NSERC) of Canada to I.R.B.

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© Springer Science+Business Media New York 2016

Authors and Affiliations

  1. 1.Department of Biological Sciences, Centre for the Neurobiology of StressUniversity of Toronto ScarboroughTorontoCanada

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