Human sat III and Drosophila hsrω transcripts: a common paradigm for regulation of nuclear RNA processing in stressed cells
Open Access
- 4 October 2006
- journal article
- review article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 34 (19) , 5508-5514
- https://doi.org/10.1093/nar/gkl711
Abstract
Exposure of cells to stressful conditions elicits a highly conserved defense mechanism termed the heat shock response, resulting in the production of specialized proteins which protect the cells against the deleterious effects of stress. The heat shock response involves not only a widespread inhibition of the ongoing transcription and activation of heat shock genes, but also important changes in post-transcriptional processing. In particular, a blockade in splicing and other post-transcriptional processing has been described following stress in different organisms, together with an altered spatial distribution of the proteins involved in these activities. However, the specific mechanisms that regulate these activities under conditions of stress are little understood. Non-coding RNA molecules are increasingly known to be involved in the regulation of various activities in the cell, ranging from chromatin structure to splicing and RNA degradation. In this review, we consider two non-coding RNAs, the hsr(omega) transcripts in Drosophila and the sat III transcripts in human cells, that seem to be involved in the dynamics of RNA-processing factors in normal and/or stressed cells, and thus provide new paradigms for understanding transcriptional and post-transcriptional regulations in normal and stressed cells.Keywords
This publication has 99 references indexed in Scilit:
- Understanding alternative splicing: towards a cellular codeNature Reviews Molecular Cell Biology, 2005
- Concepts in nuclear architectureBioEssays, 2005
- Sequestration of TRAF2 into Stress Granules Interrupts Tumor Necrosis Factor Signaling under Stress ConditionsMolecular and Cellular Biology, 2005
- Mimicking phosphorylation of the small heat‐shock protein αB‐crystallin recruits the F‐box protein FBX4 to nuclear SC35 specklesEuropean Journal of Biochemistry, 2004
- Heat stress-induced localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for αB-crystallin and Hsp25Experimental Cell Research, 2004
- Nuclear stress bodies: a heterochromatin affair?Nature Reviews Molecular Cell Biology, 2004
- Nuclear speckles: a model for nuclear organellesNature Reviews Molecular Cell Biology, 2003
- Purification and biochemical characterization of interchromatin granule clustersThe EMBO Journal, 1999
- RNA splicing: What has phosphorylation got to do with it?Current Biology, 1999
- Two major RNA products are transcribed from heat-shock locus 93D ofDrosophila melanogasterChromosoma, 1985