A Family of Human RNA-binding Proteins Related to theDrosophila Bruno Translational Regulator

Good, Peter J.; Chen, Qingdan; Warner, Stephen J.; Herring, Dina

doi:10.1074/jbc.m003083200

Cited by 131 publications

(167 citation statements)

References 80 publications

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“…This characteristic of the cis-element bound by CUG-BP is in agreement with data obtained using a tri-hybrid assay (28). In addition, in a UV cross-linking experiment, CUG-BP binds BRE sequences that consist mainly of U/purine repeats (29). It remains to be demonstrated conclusively that CUG-BP is a deadenylation factor in human cells, where it would regulate the expression of c-Jun proto-oncogene.…”

Section: Discussionmentioning

confidence: 99%

c-Jun ARE Targets mRNA Deadenylation by an EDEN-BP (Embryo Deadenylation Element-binding Protein)-dependent Pathway

Paillard

Legagneux

Maniey

et al. 2002

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

c-Jun ARE Targets mRNA Deadenylation by an EDEN-BP (Embryo Deadenylation Element-binding Protein)-dependent Pathway

Paillard

Legagneux

Maniey

et al. 2002

Journal of Biological Chemistry

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“…Six members of the CELF family have been identified in human (Good et al, 2000;Ladd et al, 2001: CUG binding protein 1 (CUG-BP1), embryonic lethal abnormal vision type RNA binding protein 3 (ETR-3), CELF3, CELF4, CELF5, and CELF6.…”

Section: Introductionmentioning

confidence: 99%

Cloning and embryonic expression patterns of the chicken CELF family

Brimacombe

Ladd

2007

Developmental Dynamics

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The CUG-BP and ETR-3-like factor (CELF) protein family has been implicated in the regulation of premRNA alternative splicing, mRNA stability, and translation. Here we discuss the evolution and radiation of the CELF protein subfamilies, and report the cloning of the chicken CELF family members. In this study, we examined the embryonic expression patterns of the CELF family in the chick by in situ hybridization. We found that the tissue specificity reported for CELF proteins in the adult is established early during embryogenesis. Members of one subfamily, CUG-BP1 and ETR-3, are broadly expressed in the early embryo, while members of the second subfamily, CELF4-6, are restricted primarily to the nervous system. Expression patterns of individual CELF genes in several tissues, including the heart, liver, eye, and neural tube, exhibit distinct, yet overlapping, expression patterns. This suggests that different members of the CELF family play distinct functional roles during embryogenesis. Developmental Dynamics 236:2216 -2224, 2007.

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“…Two neuronal nuclei-restricted RNAbinding proteins, UNC-75 and EXC-7, are required for synaptic transmission without affecting neuronal development or synaptogenesis in C. elegans (34). UNC-75 is the C. elegans ortholog of the CELF͞BrunoL family of proteins that control pre-mRNA splicing in mammals (35,36) and mediate translation repression in Drosophila oocytes (37,38). EXC-7 is the C. elegans ELAV (embryonic lethal abnormal vision)͞Hu family protein, a neuron-specific alternative splicing factor in Drosophila (39)(40)(41)(42) and neuron-specific RNA-processing regulator in mammals (43)(44)(45).…”

mentioning

confidence: 99%

The C2H2 zinc-finger protein SYD-9 is a putative posttranscriptional regulator for synaptic transmission

Wang

Gracheva

Richmond

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Communication between neurons is largely achieved through chemical synapses, where neurotransmitters are released from synaptic vesicles at presynaptic terminals to activate postsynaptic cells. Exo-and endocytosis are coordinated to replenish the synaptic vesicle pool for sustained neuronal activity. We identified syd-9 (syd, synapse defective), a gene that encodes multiple C2H2 zinc-finger domain-containing proteins specifically required for synaptic function in Caenorhabditis elegans. syd-9 loss-of-function mutants exhibit locomotory defects, a diffuse distribution of synaptic proteins, and decreased synaptic transmission with unaffected neurodevelopment. syd-9 mutants share phenotypic and ultrastructural characteristics with mutants that lack synaptic proteins that are required for endocytosis. syd-9 mutants also display genetic interactions with these endocytotic mutants, suggesting that SYD-9 regulates endocytosis. SYD-9 proteins are enriched in the nuclei of both neuron and muscle cells, but their neuronal expression plays a major role in locomotion. SYD-9 isoforms display a speckle-like expression pattern that is typical of RNAbinding proteins that regulate premRNA splicing. Furthermore, syd-9 functions in parallel with unc-75 (unc, uncoordinated), the C. elegans homologue of the CELF͞BrunoL family protein that regulates mRNA alternative splicing and processing, and is also required specifically for synaptic transmission. We propose that neuronal SYD-9 proteins are previously uncharacterized and specific posttranscriptional regulators of synaptic vesicle endocytosis.BrunoL͞UNC-75 ͉ Caenorhabditis elegans ͉ endocytosis ͉ synaptic function C hemical synapses mediate neuronal communication through the regulated release of neurotransmitters from synaptic vesicles. Extensive studies have focused on the molecular machinery that mediates and regulates exocytosis, the process in which membrane fusion between synaptic vesicles and the plasma membrane leads to neurotransmitter release and endocytosis, the process that recovers synaptic vesicles from the plasma membrane (1, 2).The release of neurotransmitters is stimulated by the influx of Ca 2ϩ at the presynaptic active zones. Protein components of the vesicle membranes (synaptobrevin, SNB) and plasma membranes [syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa)] form a SNARE complex that functions as a minimal fusion machine to drive vesicle fusion (3-5). The formation and conformational change of the SNARE complex requires modulation by other proteins (6-9). Synaptotagmin (SNT) is a vesicle membrane protein that binds to Ca 2ϩ and forms complexes with phospholipids and SNARE complexes. It is a proposed Ca 2ϩ sensor for Ca 2ϩ -dependent exocytosis (10-12). SNT-1 knockout mice display selective loss of Ca 2ϩ -triggered fast exocytosis, and loss of SNT function in Caenorhabditis elegans and Drosophila leads to a large reduction of exocytosis (13,14). Disrupting the function of UNC13͞mUNC13 and UNC-18͞mUNC18 (UNC, uncoordinated) also leads to a reduction...

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A Family of Human RNA-binding Proteins Related to theDrosophila Bruno Translational Regulator

Cited by 131 publications

References 80 publications

c-Jun ARE Targets mRNA Deadenylation by an EDEN-BP (Embryo Deadenylation Element-binding Protein)-dependent Pathway

c-Jun ARE Targets mRNA Deadenylation by an EDEN-BP (Embryo Deadenylation Element-binding Protein)-dependent Pathway

Cloning and embryonic expression patterns of the chicken CELF family

The C2H2 zinc-finger protein SYD-9 is a putative posttranscriptional regulator for synaptic transmission

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