Insights into mRNA transport in neurons

Roegiers, Fabrice

doi:10.1073/pnas.0630376100

Cited by 11 publications

(7 citation statements)

References 44 publications

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“…These include SYNCRIP (synaptotagmin-binding, cytoplasmic RNA-interacting protein), hnRNPA1 (heterogeneous nuclear ribonucleoprotein A1), Staufen, FMRP (fragile X mental retardation protein), and HuR (Hu antigen R; Atasoy et al, 1998;Peng et al, 1998;Fan and Steitz, 1998;Keene, 1999;Kohrmann et al, 1999;Brennan and Steitz, 2001;Tang et al, 2001;Mazroui et al, 2002;Belanger et al, 2003;Roegiers, 2003;VilFig. 1.…”

Section: Subset Of Astrocytoma Gwbs Containing the Proteins Syncrip mentioning

confidence: 98%

Markers of mRNA stabilization and degradation, and RNAi within astrocytoma GW bodies

Moser

Eystathioy

Chan

et al. 2007

J of Neuroscience Research

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GW bodies (GWBs) are unique cytoplasmic structures that contain the mRNA binding protein GW182 and other proteins involved in mRNA processing pathways. The rationale for this study arose from clinical studies indicating that 33% of patients with GWB autoantibodies have a motor/sensory neuropathy and/or ataxia. The novelty of this study is the identification of GWBs in astrocytes and astrocytoma cells within cell bodies and cytoplasmic projections. Astrocytoma GWBs exhibit complex heterogeneity with combinations of LSm4 and XRN1 as well as Ago2 and Dicer, key proteins involved in mRNA degradation and RNA interference, respectively. GWB subsets contained the mRNA transport and stabilization proteins SYNCRIP, hnRNPA1, and FMRP, not previously described as part of the GWB complex. Immunoprecipitation of astrocytoma GWBs suggested that Dicer, hDcp, LSm4, XRN1, SYNCRIP, and FMRP form a multiprotein complex. GWBs are likely involved in a number of regulatory mRNA pathways in astrocytes and astrocytoma cells.

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Section: Subset Of Astrocytoma Gwbs Containing the Proteins Syncrip mentioning

confidence: 98%

Markers of mRNA stabilization and degradation, and RNAi within astrocytoma GW bodies

Moser

Eystathioy

Chan

et al. 2007

J of Neuroscience Research

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“…In contrast to neuroblasts, SOP cells have two counteracting complexes, (i) G α i/Pins towards the anterior and (ii) DmPar6/DaPKC/Baz towards the posterior [ 278 ]. Furthermore, Inscuteable is not expressed in pI cells [ 279 ], and its ectopic expression reverses polarity, bringing Bazooka into the anterior complex with Pins, such that cell-fate determinants such as Numb mislocalize to the posterior [ 280 ]. Division of SOP cells is asymmetric only in the context of cell-fate determinant distribution to daughter cells, as the cells and spindle sizes are equal.…”

Section: Asymmetric Cell Division In Drosophilamentioning

confidence: 99%

G-protein signaling: back to the future

McCudden

Hains

Kimple

et al. 2005

CMLS, Cell. Mol. Life Sci.

426

335

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Abstract. Heterotrimeric G-proteins are intracellular partners of G-protein-coupled receptors (GPCRs). GPCRs act on inactive Ga·GDP/Gbg heterotrimers to promote GDP release and GTP binding, resulting in liberation of Ga from Gbg. Ga·GTP and Gbg target effectors including adenylyl cyclases, phospholipases and ion channels. Signaling is terminated by intrinsic GTPase activity of Ga and heterotrimer reformation -a cycle accelerated by 'regulators of G-protein signaling' (RGS proteins). Recent studies have identified several unconventional G-protein signaling pathways that diverge from this CMLS, Cell. Mol. Life Sci. 62 (2005) 551-577 1420-682X/05/050551-27 DOI 10.1007/s00018-004-4462-3 © Birkhäuser Verlag, Basel, 2005 CMLS Cellular and Molecular Life Sciencesstandard model. Whereas phospholipase C (PLC) b is activated by Ga q and Gbg, novel PLC isoforms are regulated by both heterotrimeric and Ras-superfamily G-proteins. An Arabidopsis protein has been discovered containing both GPCR and RGS domains within the same protein. Most surprisingly, a receptor-independent Ga nucleotide cycle that regulates cell division has been delineated in both Caenorhabditis elegans and Drosophila melanogaster. Here, we revisit classical heterotrimeric G-protein signaling and explore these new, non-canonical G-protein signaling pathways.

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“…Until now, only a few components of such RNP complexes, which are involved in RNA transport and localization in mammalian cells and, in particular, primary neurons, have been identified (Krichevsky and Kosik, 2001;Ohashi et al, 2002). The mammalian homolog of Drosophila Staufen has been implicated in RNA localization into dendrites of hippocampal neurons (Kiebler et al, 1999;Köhrmann et al, 1999a;Tang et al, 2001), and the Staufen-containing RNPs are thought to be the active transport units for dendritically localized mRNAs (Köhrmann et al, 1999a;Mallardo et al, 2003;Roegiers, 2003). Recently, protein phosphatase 1 was identified as a Staufen1 (Stau1)-interacting protein; this suggested that both proteins might be recruited into the same RNPs (Monshausen et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Barentsz, a New Component of the Staufen-Containing Ribonucleoprotein Particles in Mammalian Cells, Interacts with Staufen in an RNA-Dependent Manner

et al. 2003

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Staufen1, the mammalian homolog of Drosophila Staufen, assembles into ribonucleoprotein particles (RNPs), which are thought to transport and localize RNA into dendrites of mature hippocampal neurons. We therefore investigated whether additional components of the RNA localization complex besides Staufen are conserved. One candidate is the mammalian homolog of Drosophila Barentsz (Btz), which is essential for the localization of oskar mRNA to the posterior pole of the Drosophila oocyte and is a component of the oskar RNA localization complex along with Staufen. In this study, we report the characterization of mammalian Btz, which behaves like a nucleocytoplasmic shuttling protein. When expressed in the Drosophila egg chamber, mammalian Btz is still able to interact with Drosophila Staufen and reach the posterior pole in the wild-type oocyte, but does not rescue the btz mutant phenotype. Most interestingly, we show by immunoprecipitation assays that Btz interacts with mammalian Staufen in an RNA-dependent manner through a conserved domain, which encompasses the region of homology to the Drosophila Btz protein and contains a novel conserved motif. One candidate for an RNA that mediates this interaction is the dendritically localized brain cytoplasmic 1 transcript. In addition, Btz and Staufen1 colocalize within particles in the cell body and, to a more variable extent, in dendrites of mature hippocampal neurons. Together, our data suggest that the mRNA transport machinery is conserved during evolution, and that mammalian Btz is an additional component of the dendritic RNPs in hippocampal neurons.

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Insights into mRNA transport in neurons

Cited by 11 publications

References 44 publications

Markers of mRNA stabilization and degradation, and RNAi within astrocytoma GW bodies

Markers of mRNA stabilization and degradation, and RNAi within astrocytoma GW bodies

G-protein signaling: back to the future

Barentsz, a New Component of the Staufen-Containing Ribonucleoprotein Particles in Mammalian Cells, Interacts with Staufen in an RNA-Dependent Manner

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