RNA-mediated response to heat shock in mammalian cells

Shamovsky, Ilya; Ivannikov, Maxim V.; Kandel, Eugene; Gershon, David; Nudler, Evgeny

doi:10.1038/nature04518

Cited by 327 publications

(258 citation statements)

References 30 publications

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“…Evf-2 thus appears to be acting at least partially as a RNA-based transcriptional coactivator. This potential function is not unprecedented, as the ncRNA SRA has been known for some time to act as a transcriptional coactivator by directly interacting with steroid receptors (Lanz et al, 1999), while the ncRNAs NRSE and HSR have been shown to regulate the activity of REST and HSF-1, respectively (Kuwabara et al, 2004;Shamovsky et al, 2006). However, the story is likely more complex for Evf-2.…”

Section: How Might Osts Work?mentioning

confidence: 99%

New meaning in the message: Noncoding RNAs and their role in retinal development

Rapicavoli

Blackshaw

2009

Developmental Dynamics

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Recent studies have indicated that non-protein-coding RNAs (ncRNAs) may play prominent and diverse roles in the development of the nervous system. These ncRNAs are now known to perform a broad range of cellular functions, and in particular appear to be prominent players in the regulation of transcription and translation. In this review, we discuss recent advances in our understanding of the role of ncRNAs in vertebrate retinal development. Noncoding RNAs that are known or suspected to play a functional role in the specification and maturation of retinal cell subtypes include miRNAs, long noncoding opposite-strand transcripts (OSTs), and other long ncRNAs such as Tug1 and RNCR2. Though the mechanism of action of most of these ncRNAs is still largely unclear, it is likely that these molecules represent a major, and thus far largely unappreciated, component of the molecular machinery involved in retinal cell fate specification.

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Section: How Might Osts Work?mentioning

confidence: 99%

New meaning in the message: Noncoding RNAs and their role in retinal development

Rapicavoli

Blackshaw

2009

Developmental Dynamics

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“…Upon stress, HSF1 becomes trimerized, binds to the heat-shock elements present in the HSP promoters, and rescues the RNA pol II elongation complex from promoter-proximal arrest (Shopland et al 1995;Shopland and Lis 1996). A recent study has shown that HSF1 activation by heat shock is an active process and is mediated by a ribonucleoprotein complex containing translation elongation factor eEF1A and a newly identified ncRNA, HSR-1 (Shamovsky et al 2006). HSR-1 RNA is an ∼600-nt poly(A) − RNA and shows a high degree of homology between human and rodents.…”

Section: Heat Shock Rna-1 (Hsr-1)mentioning

confidence: 99%

Eukaryotic regulatory RNAs: an answer to the ‘genome complexity’ conundrum

Prasanth¹,

Spector²

2007

Genes Dev.

365

305

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A large portion of the eukaryotic genome is transcribed as noncoding RNAs (ncRNAs). While once thought of primarily as "junk," recent studies indicate that a large number of these RNAs play central roles in regulating gene expression at multiple levels. The increasing diversity of ncRNAs identified in the eukaryotic genome suggests a critical nexus between the regulatory potential of ncRNAs and the complexity of genome organization. We provide an overview of recent advances in the identification and function of eukaryotic ncRNAs and the roles played by these RNAs in chromatin organization, gene expression, and disease etiology.

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“…37,38 Upregulation of EF1α has been associated with cell death. 38,39 Our finding that HDM2 interacts with EF1α suggests that they may modulate each others function. A recent publication 39 described a role of EF1α in activation of a transcription factor heat shock factor 1 (HSF1).…”

Section: Resultsmentioning

confidence: 96%

HDM2-Binding Partners: Interaction with Translation Elongation Factor EF1α

et al. 2007

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To understand the cellular functions of HDM2, we attempted to identify novel HDM2-interacting proteins by proteomic analysis. Along with previously identified interactions with the ribosomal proteins, our analysis reveals interactions of HDM2 with the ribosomal translation elongation factor EF1α, 40S ribosomal protein S20, tubulins, glyceraldehyde 3-phosphate dehydrogenase, and a proteolysis-inducing factor dermicidin in the absence of tumor suppressor p53. Because a CTCL tumor antigen HD-CL-08 has high degree of homology with EF1α, we confirmed interaction of HDM2 with EF1α by immunoprecipitation and Western blot analysis in transformed as well as near normal diploid cells. Endogenous HDM2-EF1α complex was detected in cancer cells overexpressing HDM2, suggesting a possible role of this interaction in HDM2-mediated oncogenesis. Consistent with their interaction, colocalization of HDM2 and EF1α can be detected in the cytoplasm of normal or transformed cells. Amino acid residues 1-58 and 221-325 of HDM2 were found to be essential for its interaction with EF1α, suggesting that the interaction is independent of its other ribosomal interacting proteins L5, L11, and L23. Overexpression of HDM2 did not affect translation. Because EF1α has been implicated in DNA replication and severing of microtubules, interaction of HDM2 with EF1α may signify a p53-independent cell growth regulatory role of HDM2.

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RNA-mediated response to heat shock in mammalian cells

Cited by 327 publications

References 30 publications

New meaning in the message: Noncoding RNAs and their role in retinal development

New meaning in the message: Noncoding RNAs and their role in retinal development

Eukaryotic regulatory RNAs: an answer to the ‘genome complexity’ conundrum

HDM2-Binding Partners: Interaction with Translation Elongation Factor EF1α

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