Tissue development and RNA control: “HOW” is it coordinated?

Volk, Talila; Israeli, David; Nir, Ronit; Toledano, Hila

doi:10.1016/j.tig.2007.11.009

Cited by 42 publications

(44 citation statements)

References 71 publications

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“…Cbr-gld-1 alleles nm41 and nm64 were recognized by sterile F 2 progeny of ethyl methanesulfonate -mutagenized AF16 animals, as previously described (27). Cbr-gld-1(nm68) was identified in PCR-based deletion screens (12).…”

Section: Methodsmentioning

confidence: 99%

“…STAR proteins are implicated in diverse cellular processes, including cell division, gametogenesis, apoptosis, and embryonic and larval development, and are found across the Metazoa (e.g., refs. [23][24][25][26][27]. C. elegans GLD-1 is a germ-line-specific, pleiotropic translational repressor (22,28,29) required for the mitosis/meiosis decision of germ-line stem cells, meiotic progression of oocyte-fated cells, and specification of C. elegans hermaphrodite sperm in an otherwise female body (30,31).…”

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confidence: 99%

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Independent recruitments of a translational regulator in the evolution of self-fertile nematodes

Beadell

Liu²,

Johnson³

et al. 2011

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

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Pleiotropic developmental regulators have been repeatedly linked to the evolution of anatomical novelties. Known mechanisms include cis-regulatory DNA changes that alter regulator transcription patterns or modify target-gene linkages. Here, we examine the role of another form of regulation, translational control, in the repeated evolution of self-fertile hermaphroditism in Caenorhabditis nematodes. Caenorhabditis elegans hermaphrodites initiate spermatogenesis in an otherwise female body through translational repression of the gene tra-2. This repression is mediated by GLD-1, an RNA-binding protein also required for oocyte meiosis and differentiation. By contrast, we show that in the convergently hermaphroditic Caenorhabditis briggsae, GLD-1 acts to promote oogenesis. The opposite functions of gld-1 in these species are not gene-intrinsic, but instead result from the unique contexts for its action that evolved in each. In C. elegans, GLD-1 became essential for promoting XX spermatogenesis via changes in the tra-2 mRNA and evolution of the species-specific protein FOG-2. C. briggsae GLD-1 became an essential repressor of sperm-promoting genes, including Cbr-puf-8, and did not evolve a strong association with tra-2. Despite its variable roles in sex determination, the function of gld-1 in female meiotic progression is ancient and conserved. This conserved role may explain why gld-1 is repeatedly recruited to regulate hermaphroditism. We conclude that, as with transcription factors, spatially localized translational regulators play important roles in the evolution of anatomical novelties.germ cells | translation | breeding systems | mutant

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Independent recruitments of a translational regulator in the evolution of self-fertile nematodes

Beadell

Liu²,

Johnson³

et al. 2011

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

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“…Sam68 belongs to the signal transduction and activation of RNA (STAR) family of RNA-binding proteins (RBPs). This evolutionary conserved group of proteins plays roles in cell proliferation and differentiation, which affect key developmental processes (Vernet & Artzt 1997, Volk et al 2008. STAR proteins owe their name to the presence of a structural domain for the binding of RNA, the GRP33/SAM68/GLD-1 (GSG) domain, flanked by regulatory regions containing motifs for protein-protein interactions and residues that are modified posttranslationally (Sette 2010).…”

Section: Introductionmentioning

confidence: 99%

The RNA-binding protein Sam68 is a multifunctional player in human cancer

Bielli

Busà

Paronetto

et al. 2011

Endocrine-Related Cancer

148

145

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Src associated in mitosis, of 68 kDa (Sam68) is a KH domain RNA-binding protein that belongs to the signal transduction and activation of RNA family. Although ubiquitously expressed, Sam68 plays very specialized roles in different cellular environments. In most cells, Sam68 resides in the nucleus and is involved in several steps of mRNA processing, from transcription, to alternative splicing, to nuclear export. In addition, Sam68 translocates to the cytoplasm upon cell stimulation, cell cycle transitions or viral infections, where it takes part to signaling complexes and associates with the mRNA translation machinery. Recent evidence has linked Sam68 function to the onset and progression of endocrine tumors, such as prostate and breast carcinomas. Notably, all the biochemical activities reported for Sam68 seem to be implicated in carcinogenesis. Herein, we review the recent advancement in the knowledge of Sam68 function and regulation and discuss it in the frame of its participation to neoplastic transformation and tumor progression.

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“…The short isoform, HOW(S), binds Crn in the cytoplasm and is able to shuttle to the nucleus. The long isoform, HOW(L), is only found in the nucleus and cannot bind Crn (Edenfeld et al, 2006;Volk et al, 2008). The middle form is predicted by FlyBase and is currently not further analyzed.…”

Section: Introductionmentioning

confidence: 99%

The regulation of glial-specific splicing ofNeurexin IVrequires HOW and Cdk12 activity

2012

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SUMMARYThe differentiation of the blood-brain barrier (BBB) is an essential process in the development of a complex nervous system and depends on alternative splicing. In the fly BBB, glial cells establish intensive septate junctions that require the cell-adhesion molecule Neurexin IV. Alternative splicing generates two different Neurexin IV isoforms: Neurexin IV exon3 , which is found in cells that form septate junctions, and Neurexin IV exon4 , which is found in neurons that form no septate junctions. Here, we show that the formation of the BBB depends on the RNA-binding protein HOW (Held out wings), which triggers glial specific splicing of Neurexin IV exon3 . Using a set of splice reporters, we show that one HOW-binding site is needed to include one of the two mutually exclusive exons 3 and 4, whereas binding at the three further motifs is needed to exclude exon 4. The differential splicing is controlled by nuclear access of HOW and can be induced in neurons following expression of nuclear HOW. Using a novel in vivo two-color splicing detector, we then screened for genes required for full HOW activity. This approach identified Cyclin-dependent kinase 12 (Cdk12) and the splicesosomal component Prp40 as major determinants in regulating HOWdependent splicing of Neurexin IV. Thus, in addition to the control of nuclear localization of HOW, the phosphorylation of the Cterminal domain of the RNA polymerase II by Cdk12 provides an elegant mechanism in regulating timed splicing of newly synthesized mRNA molecules.

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Tissue development and RNA control: “HOW” is it coordinated?

Cited by 42 publications

References 71 publications

Independent recruitments of a translational regulator in the evolution of self-fertile nematodes

Independent recruitments of a translational regulator in the evolution of self-fertile nematodes

The RNA-binding protein Sam68 is a multifunctional player in human cancer

The regulation of glial-specific splicing ofNeurexin IVrequires HOW and Cdk12 activity

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