Faculty Opinions recommendation of Nuclear transit of the RNA-binding protein She2 is required for translational control of localized ASH1 mRNA.

AbstractSurvival of all living organisms requires the ability to detect attack and swiftly counter with protective immune responses. Despite considerable mechanistic advances, interconnectivity of signaling circuits often remains unclear. A newly-characterized protein, IMMUNOREGULATORY RNA-BINDING PROTEIN (IRR), negatively regulates immune responses in both maize and Arabidopsis, with disrupted function resulting in enhanced disease resistance. IRR physically interacts with, and promotes canonical splicing of, transcripts encoding defense signaling proteins, including the key negative regulator of pattern recognition receptor signaling complexes, CALCIUM-DEPENDENT PROTEIN KINASE 28 (CPK28). Upon immune activation by Plant Elicitor Peptides (Peps), IRR is dephosphorylated, disrupting interaction withCPK28transcripts and resulting in accumulation of an alternative splice variant encoding a truncated CPK28 protein with impaired kinase activity and diminished function as a negative regulator. We demonstrate a novel circuit linking Pep-induced post-translational modification of IRR with post-transcriptionally-mediated attenuation of CPK28 function to dynamically amplify Pep signaling and immune output.One Sentence SummaryPlant innate immunity is promoted by post-translational modification of a novel RNA-binding protein that regulates alternative splicing of transcripts encoding defense signaling proteins to dynamically increase immune receptor signaling capacity through deactivation of a key signal-buffering circuit.

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

Molecular Biology of the Cell ◽

10.1091/mbc.e05-06-0548 ◽

2006 ◽

Vol 17 (1) ◽

pp. 14-24 ◽

Cited By ~ 60

Author(s):

Maria Paola Paronetto ◽

Francesca Zalfa ◽

Flavia Botti ◽

Raffaele Geremia ◽

Claudia Bagni ◽

...

Keyword(s):

Translational Control ◽

Rna Binding ◽

Rna Binding Proteins ◽

Binding Protein ◽

Rna Binding Protein ◽

Male Meiosis ◽

Binding Motif ◽

Mitogen Activated Protein ◽

Pachytene Spermatocytes ◽

And Function

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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Spnr, a murine RNA-binding protein that is localized to cytoplasmic microtubules.

The Journal of Cell Biology ◽

10.1083/jcb.129.4.1023 ◽

1995 ◽

Vol 129 (4) ◽

pp. 1023-1032 ◽

Cited By ~ 67

Author(s):

J M Schumacher ◽

K Lee ◽

S Edelhoff ◽

R E Braun

Keyword(s):

Translational Control ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Translational Repression ◽

Rna Transport ◽

Binding Domains ◽

Cytoplasmic Microtubules ◽

Pachytene Spermatocytes ◽

Expression Libraries

Previous studies in transgenic mice have established the importance of the 3' untranslated region (UTR) of the spermatid-specific protamine-1 (Prm-1) mRNA in its translational control during male germ cell development. To clone genes that mediate the translational repression or activation of the Prm-1 mRNA, we screened cDNA expression libraries made with RNA from pachytene spermatocytes and round spermatids, with an RNA probe corresponding to the 3' UTR of Prm-1. We obtained six independent clones that encode Spnr, a spermatid perinuclear RNA-binding protein. Spnr is a 71-kD protein that contains two previously described RNA binding domains. The Spnr mRNA is expressed at high levels in the testis, ovary, and brain, and is present in multiple forms in those tissues. Immunolocalization of the Spnr protein within the testis shows that it is expressed exclusively in postmeiotic germ cells and that it is localized to the manchette, a spermatid-specific microtubular array. Although the Spnr protein is expressed too late to be directly involved in the translational repression of Prm-1 specifically, we suggest that the Spnr protein may be involved in other aspects of spermatid RNA metabolism, such as RNA transport or translational activation.

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Cbk1 Regulation of the RNA-Binding Protein Ssd1 Integrates Cell Fate with Translational Control

Current Biology ◽

10.1016/j.cub.2009.10.071 ◽

2009 ◽

Vol 19 (24) ◽

pp. 2114-2120 ◽

Cited By ~ 62

Author(s):

Jaclyn M. Jansen ◽

Antony G. Wanless ◽

Christopher W. Seidel ◽

Eric L. Weiss

Keyword(s):

Cell Fate ◽

Translational Control ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein

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Xenopus laevis zygote arrest 2 (zar2) encodes a zinc finger RNA-binding protein that binds to the translational control sequence in the maternal Wee1 mRNA and regulates translation

Developmental Biology ◽

10.1016/j.ydbio.2012.06.012 ◽

2012 ◽

Vol 369 (2) ◽

pp. 177-190 ◽

Cited By ~ 15

Author(s):

Amanda Charlesworth ◽

Tomomi M. Yamamoto ◽

Jonathan M. Cook ◽

Kevin D. Silva ◽

Cassandra V. Kotter ◽

...

Keyword(s):

Xenopus Laevis ◽

Zinc Finger ◽

Translational Control ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Control Sequence

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The RNA-binding protein PTB exerts translational control on 3′-untranslated region of the mRNA for the ATP synthase β-subunit

Biochemical and Biophysical Research Communications ◽

10.1016/j.bbrc.2007.04.088 ◽

2007 ◽

Vol 357 (4) ◽

pp. 1107-1112 ◽

Cited By ~ 7

Author(s):

Raquel Reyes ◽

José M. Izquierdo

Keyword(s):

Atp Synthase ◽

Translational Control ◽

Untranslated Region ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Β Subunit

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149. TRANSLATIONAL CONTROL IN FOLLICULOGENESIS AND OOCYTE DEVELOPMENT: A ROLE FOR RNA-BINDING PROTEIN MUSASHI-1

Reproduction Fertility and Development ◽

10.1071/srb10abs149 ◽

2010 ◽

Vol 22 (9) ◽

pp. 67

Author(s):

K. M. Gunter ◽

B. A. Fraser ◽

A. P. Sobinoff ◽

V. Pye ◽

N. A. Siddall ◽

...

Keyword(s):

Translational Control ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Oocyte Development ◽

Cell Cycle Regulators ◽

Translational Repressor ◽

Qpcr Analysis ◽

Mrna Pool ◽

Rna Immunoprecipitation

Control of the maternal mRNA pool during oocyte maturation is crucial to the correct temporal and spatial expression of proteins, particularly during oocyte transcriptional quiescence. We have identified Musashi-1 as being present within the oocyte/ovary, where this RNA-binding protein is believed to act as a translational repressor of target mRNAs. Recent studies in mammalian neural and intestinal systems have identified a number of cell cycle regulators as potential targets of Msi-1. Using Msi-1 protein-RNA immunoprecipitation, we have also identified musashi-2 (msi-2) and c-mos as putative targets in the mouse oocyte. To further study these targets, a transgenic mouse was produced to overexpress Msi-1 exclusively in the oocyte. QPCR analysis, performed on intact ovaries of wild type (WT) and Tg mice, confirmed a 1.5-fold increase in msi-1 expression in tgMsi-1/+ ovaries in excess of WT ovary expression. QPCR analysis of Msi-1 target expression, performed on intact WT and Tg ovaries, in conjunction with transcript obtained from the Msi-1 protein-RNA immunoprecipitation, revealed an overall increase in expression in the tgMsi-1/+ and Msi-1 IP samples, respectively, of p21WAF-1 (~2.5-fold; undetected), cdkn2a (~2-fold; undetected), notch1 (~3-fold;undetected), c-mos (no difference; ~41-fold) and msi-2 (~7-fold; ~10-fold). Immunohistochemical analysis of Msi-2 protein expression in transgenic juvenile mouse ovaries,demonstrated a decrease in expression of Msi-2 in tgMsi-1/+ ovaries, when compared to WT ovary expression, suggesting that Msi-2 mRNA is translationally repressed by Msi-1. Therefore, preliminary analysis suggests that Msi-1 may play a role inregulating transcripts of genes necessary for processes characteristic of meiotic progression and oocyte development.

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