STAR, a gene family involved in signal transduction and activation of RNA

Vernet, Corine; Artzt, Karen

doi:10.1016/s0168-9525(97)01269-9

Cited by 278 publications

(255 citation statements)

References 58 publications

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“…25 Sam68 belongs to a class of RNAbinding proteins (STAR, signal transduction and RNA metabolism) that appear to link activation of signal transduction pathways to translational regulation of target mRNAs. 26 Indeed, STAR proteins act as translational repressors and phosphorylation modifies their subcellular localization and RNA affinity. 26 In particular, Sam68 was shown to play a scaffold role in Src kinase-activated pathways, 16,27 and tyrosine phosphorylation of Sam68 by Src kinases triggers the release of bound RNA and might allow translational activation.…”

Section: Discussionmentioning

confidence: 99%

Expression of a Truncated Form of the c-Kit Tyrosine Kinase Receptor and Activation of Src Kinase in Human Prostatic Cancer

Paronetto

Farini

Sammarco

et al. 2004

The American Journal of Pathology

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The c-Kit receptor belongs to type III tyrosine kinase receptor, which consists of an extracellular ligand binding domain and an intracellular kinase domain. In the kinase domain, the ATP binding site is separated from the phosphotransferase site by an interkinase sequence required for interaction with signal transduction proteins involved in the c-Kit pathway. 1 The c-Kit receptor is expressed in a wide variety of normal and neoplastic tissues. A positive correlation between misregulation of the c-kit gene and malignant transformation of cells has been reported. 2,3 For instance, substitution mutations in exon 11 of the gene, changing amino acids of the juxtamembrane region of the receptor, are associated with gastrointestinal stromal tumors, whereas mutations in exon 17 that substitute Asp816, just downstream of the tyrosine kinase signature, are associated with myeloid leukemias and testicular seminomas. 2,3 These mutations induce ligand-independent dimerization or autophosphorylation of the receptor and they cause constitutive activation of downstream signaling pathways. Moreover, overexpression of c-Kit and its ligand SCF occurs in several tumors and they probably stimulate proliferation in an autocrine or paracrine manner. 2 Recently, c-kit expression in various tumors has been revisited because this receptor is a target of the anti-cancer activity of a well described tyrosine kinase inhibitor: imatinib (STI1571). 2,4 Beside mutations affecting the activity of the full-length c-Kit, expression of an alternative transcript of human c-kit has been described in several transformed cell lines. The

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Section: Discussionmentioning

confidence: 99%

Expression of a Truncated Form of the c-Kit Tyrosine Kinase Receptor and Activation of Src Kinase in Human Prostatic Cancer

Paronetto

Farini

Sammarco

et al. 2004

The American Journal of Pathology

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“…An emerging class of proteins involved in RNA homeostasis is represented by the STAR (signal transduction and activation of RNA metabolism) family (Vernet and Artzt, 1997). STAR proteins are conserved across eukaryotes and may represent a direct link between signal transduction pathways and RNA metabolism.…”

Section: Introductionmentioning

confidence: 99%

“…STAR proteins are conserved across eukaryotes and may represent a direct link between signal transduction pathways and RNA metabolism. They bind RNA through a GSG (Grp33/Sam68/GLD-1) domain, which contains a single KH domain (hnRNP K homology domain) flanked by conserved N-and C-terminal sequences named QUA1 and QUA2 domains required for homodimerization and specificity in RNA binding (Vernet and Artzt, 1997;Lukong and Richard, 2003). Interestingly, GLD-1, a STAR protein of C. elegans, is a temporal regulator of sexual identity and it is necessary for meiotic prophase progression of germ cells (Francis et al, 1995;Jan et al, 1999;Goodwin and Ellis, 2002).…”

Section: Introductionmentioning

confidence: 99%

The Nuclear RNA-binding Protein Sam68 Translocates to the Cytoplasm and Associates with the Polysomes in Mouse Spermatocytes

Paronetto

Zalfa

Botti

et al. 2006

MBoC

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Translational control plays a crucial role during gametogenesis in organisms as different as worms and mammals. Mouse knockout models have highlighted the essential function of many RNA-binding proteins during spermatogenesis. Herein we have investigated the expression and function during mammalian male meiosis of Sam68, an RNA-binding protein implicated in several aspects of RNA metabolism. Sam68 expression and localization within the cells is stage specific: it is expressed in the nucleus of spermatogonia, it disappears at the onset of meiosis (leptotene/zygotene stages), and it accumulates again in the nucleus of pachytene spermatocytes and round spermatids. During the meiotic divisions, Sam68 translocates to the cytoplasm where it is found associated with the polysomes. Translocation correlates with serine/ threonine phosphorylation and it is blocked by inhibitors of the mitogen activated protein kinases ERK1/2 and of the maturation promoting factor cyclinB-cdc2 complex. Both kinases associate with Sam68 in pachytene spermatocytes and phosphorylate the regulatory regions upstream and downstream of the Sam68 RNA-binding motif. Molecular cloning of the mRNAs associated with Sam68 in mouse spermatocytes reveals a subset of genes that might be posttranscriptionally regulated by this RNA-binding protein during spermatogenesis. We also demonstrate that Sam68 shuttles between the nucleus and the cytoplasm in secondary spermatocytes, suggesting that it may promote translation of specific RNA targets during the meiotic divisions.

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“…SNBs are the sites of accumulation of Sam68 (Src activated during mitosis), SLM-1, and SLM-2, three members of the family of RNA binding proteins characterized by the GSG (GRP33, Sam68, GLD-1) domain, also termed signal transduction and activation of RNA domain (Chen et al, 1997;Vernet and Artzt, 1997;Chen et al, 1999;Venables et al, 1999). The importance of SNBs is suggested by the role of Sam68 in cell cycle progression (Barlat et al, 1997), RNA export (Reddy et al, 2000), and splicing (Stoss et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Stress-induced Nuclear Bodies Are Sites of Accumulation of Pre-mRNA Processing Factors

Denegri

Chiodi

Corioni

et al. 2001

MBoC

155

143

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Heterogeneous nuclear ribonucleoprotein (hnRNP) HAP (hnRNP A1 interacting protein) is a multifunctional protein with roles in RNA metabolism, transcription, and nuclear structure. After stress treatments, HAP is recruited to a small number of nuclear bodies, usually adjacent to the nucleoli, which consist of clusters of perichromatin granules and are depots of transcripts synthesized before stress. In this article we show that HAP bodies are sites of accumulation for a subset of RNA processing factors and are related to Sam68 nuclear bodies (SNBs) detectable in unstressed cells. Indeed, HAP and Sam68 are both present in SNBs and in HAP bodies, that we rename "stress-induced SNBs." The determinants required for the redistribution of HAP lie between residue 580 and 788. Different portions of this region direct the recruitment of the green fluorescent protein to stress-induced SNBs, suggesting an interaction of HAP with different components of the bodies. With the use of the 580 -725 region as bait in a two-hybrid screening, we have selected SRp30c and 9G8, two members of the SR family of splicing factors. Splicing factors are differentially affected by heat shock: SRp30c and SF2/ASF are efficiently recruited to stress-induced SNBs, whereas the distribution of SC35 is not perturbed. We propose that the differential sequestration of splicing factors could affect processing of specific transcripts. Accordingly, the formation of stress-induced SNBs is accompanied by a change in the splicing pattern of the adenovirus E1A transcripts.

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STAR, a gene family involved in signal transduction and activation of RNA

Cited by 278 publications

References 58 publications

Expression of a Truncated Form of the c-Kit Tyrosine Kinase Receptor and Activation of Src Kinase in Human Prostatic Cancer

Expression of a Truncated Form of the c-Kit Tyrosine Kinase Receptor and Activation of Src Kinase in Human Prostatic Cancer

The Nuclear RNA-binding Protein Sam68 Translocates to the Cytoplasm and Associates with the Polysomes in Mouse Spermatocytes

Stress-induced Nuclear Bodies Are Sites of Accumulation of Pre-mRNA Processing Factors

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