REREa/Atrophin‐2 interacts with histone deacetylase and Fgf8 signaling to regulate multiple processes of zebrafish development

Plaster, Nikki; Sonntag, Carmen; Schilling, Thomas F.; Hammerschmidt, Matthias

doi:10.1002/dvdy.21196

Cited by 49 publications

(55 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Finally, Hdac1 has also been implicated in the regulation of developmental signalling cascades such as Hedgehog and Fgf8 during embryonic neurogenesis (Cunliffe, 2004;Cunliffe and Casaccia-Bonnefil, 2006;Plaster et al, 2007). Plaster and colleagues provided evidence for an in vivo function of REREa/ Hdac-mediated transcriptional repression in promoting Fgf signalling, thereby patterning the telencephalon and maintaining the midbrain-hindbrain boundary (Plaster et al, 2007).…”

Section: Hdac1 and Hdac2 In Heart Developmentmentioning

confidence: 99%

“…Plaster and colleagues provided evidence for an in vivo function of REREa/ Hdac-mediated transcriptional repression in promoting Fgf signalling, thereby patterning the telencephalon and maintaining the midbrain-hindbrain boundary (Plaster et al, 2007). Cunliffe and Casaccia identified Hdac1 as an essential factor for differentiation of neuronal precursor cells to oligodendrocytes by facilitating hedgehog-mediated expression of the oligodendrocyte marker olig2.…”

Section: Hdac1 and Hdac2 In Heart Developmentmentioning

confidence: 99%

See 1 more Smart Citation

Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation

Brunmeir¹,

Lagger²,

Seiser³

2009

Int. J. Dev. Biol.

154

147

View full text Add to dashboard Cite

During development from the fertilized egg to a multicellular organism, cell fate decisions have to be taken and cell lineage or tissue-specific gene expression patterns are created and maintained. These alterations in gene expression occur in the context of chromatin structure and are controlled by chromatin modifying enzymes. Gene disruption studies in different genetic systems have shown an essential role of various histone deacetylases (HDACs) during early development and cellular differentiation. In this review, we focus on the functions of the class I enzymes HDAC1 and HDAC2 during development in different organisms and summarise the current knowledge about their involvement in neurogenesis, myogenesis, haematopoiesis and epithelial cell differentiation. KEY WORDS: HDAC1, HDAC2, chromatin, differentiation, development Histone deacetylasesPosttranslational modifications of histones cause changes in the accessibility of DNA, thereby regulating many important cellular processes including transcription. Acetylation of core histones leads to a change in the net positive charge of histone tails and local opening of chromatin structure, a feature of transcriptionally active genes. On the other hand, deacetylated histone tails interact more closely with DNA and lead to a repressive state. Histone deacetylases (HDACs) catalyse the removal of acetyl groups from histone tails and are therefore considered as transcriptional corepressors. In addition to histones, HDACs also deacetylate non-histone proteins, such as the cytoskeletal protein tubulin (Hubbert et al., 2002) or transcription factors including p53 (Luo et al., 2000), E2F1 (MartinezBalbas et al., 2000) and YY1 (Yao et al., 2001). In fact, phylogenetic analysis suggests that the enzymatic activity was initially directed against non-histone proteins in a common ancestor devoid of histones (Gregoretti et al., 2004). In mammals, 18 deacetylases have been identified so far. These enzymes have been divided into 4 classes based on sequence similarity: Classic HDACs comprise class I (Saccharomyces cerevisiae Rpd3-like), class II (Saccharomyces cerevisiae Hda1-like) and class IV (HDAC11-like) enzymes. Class III consists of NAD-dependent, functionally unrelated Sir2-like deacetylases Int. J. Dev. Biol. 53: 275-289 (2009) Abbreviations used in this paper: HAT, histone acetyltransferase; HDA, HDAC, histone deacetylase; HDI, HDAC inhibitor; NuRD, nucleosome remodelling and deacetylase complex; Rpd3, reduced potassium dependency 3.named "sirtuins". Class I, II and IV HDACs are members of an ancient enzyme family, highly conserved throughout eukaryotic and prokaryotic evolution and are found in animals, plants, fungi, archaebacteria and eubacteria (Gregoretti et al., 2004). Class I histone deacetylasesPhylogenetic analysis revealed that class I genes in animals can be grouped into HDAC1/HDAC2, HDAC3 and HDAC8-like genes. Members of each subclass have been identified in protostomia (Oger et al., 2008) and deuterostomia. Species analysed so far carry orthologs (...

show abstract

Section: Hdac1 and Hdac2 In Heart Developmentmentioning

confidence: 99%

Section: Hdac1 and Hdac2 In Heart Developmentmentioning

confidence: 99%

Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation

Brunmeir¹,

Lagger²,

Seiser³

2009

Int. J. Dev. Biol.

154

147

View full text Add to dashboard Cite

show abstract

“…One possible explanation for the distinct effects of different Atr isoforms on migration and orientation is that although Atr2L acts to limit migration and orientation, this effect is opposed by the short isoforms, Atr1 and Atr2S. The short isoforms lack the N-terminal domains that interact with histone deacetylases (21,22,32) and conceivably could interfere with gene repression mediated by long forms of Atr (19,36). Such a model is compelling in part given the preferential induction of the short isoforms by promigratory growth factors and by arterial injury (Fig.…”

Section: Discussionmentioning

confidence: 99%

Atrophin Proteins Interact with the Fat1 Cadherin and Regulate Migration and Orientation in Vascular Smooth Muscle Cells

Hou

Sibinga

2009

Journal of Biological Chemistry

View full text Add to dashboard Cite

Fat1, an atypical cadherin induced robustly after arterial injury, has significant effects on mammalian vascular smooth muscle cell (VSMC) growth and migration. The related Drosophila protein Fat interacts genetically and physically with Atrophin, a protein essential for development and control of cell polarity. We hypothesized that interactions between Fat1 and mammalian Atrophin (Atr) proteins might contribute to Fat1 effects on VSMCs. Like Fat1, mammalian Atr expression increased after arterial injury and in VSMCs stimulated with growth and chemotactic factors including angiotensin II, basic fibroblast growth factor, and platelet-derived growth factor BB. Two distinct Atr2 transcripts, atr2L and atr2S, were identified by Northern analysis; in VSMCs, atr2S mRNA expression was more responsive to stimuli. By immunocytochemistry, Fat1 and Atrs colocalized at cell-cell junctions, in the perinuclear area, and in the nucleus. In coimmunoprecipitation studies, Fat1 interacted with both Atr1 and Atr2; these interactions required Fat1 amino acids 4300 -4400 and an intact Atro-box in the Atrs. Knockdown of Atrs by small interfering RNA did not affect VSMC growth but had complex effects on migration, which was impaired by Atr1 knockdown, enhanced by Atr2L knockdown, and unchanged when both Atr2S and Atr2L were depleted. Enhanced migration caused by Atr2L knockdown required Fat1 expression. Similarly, orientation of cells after monolayer denudation was impaired in cells with Atr1 knockdown but enhanced in cells selectively depleted of Atr2L. Together these findings suggest that Fat1 and Atrs act in concert after vascular injury but show further that distinct Atr isoforms have disparate effects on VSMC directional migration.Migration and proliferation of VSMCs 2 in the wall of injured blood vessels are critical activities in the pathogenesis of atherosclerosis and related, clinically important vascular diseases.Arterial injury strongly induces expression of the Fat1 cadherin, which has distinct effects on VSMC migration and proliferation (1). Fat1 and related, atypical cadherins form a subfamily characterized by large extracellular domains containing 34 cadherin motifs, a variable number of EGF repeats, one or two laminin A/G domains, and a single transmembrane domain (2). In vertebrates, the Fat subfamily consists of four members, Fat1, -2, -3, and -4 (or Fat-J), whereas in Drosophila, two members, Fat and Fat-like, have been identified (2, 3). Although the Drosophila fat (ft) mutation, which causes enlargement of all larval imaginal discs, including wing, leg, eye-antenna, haltere, and genital imaginal discs, was first described by Mohr 85 years ago (4), understanding of how Fat proteins control developmental processes has only recently started to emerge.Distinct functions have been ascribed to Drosophila Fat and Fat-like. The former acts as a suppressor of hyperplastic growth, as mentioned above, and as a mediator of planar cell polarity signals in development (4, 5). Fat has been identified in several recent studies as...

show abstract

“…In F6, whose phenotype has been described, we found the compound heterozygous mutations c.4264G.A (p.1422V.M) and c.3686G.A (p.1229R.Q) in RERE (MIM 605226, ENST00000337907). Homozygous mouse knockouts develop asymmetrically and have cardiovascular defects, while homozygous zebrafish mutants have various defects including abnormal fins and brains (28)(29)(30). In total we have identified two genes with de novo variants and one gene with inherited variants that could possibly account for the phenotype in F6.…”

Section: Inherited Recessive and X-linked Snvs And Indelsmentioning

confidence: 99%

2.3 Exome sequencing improves genetic diagnosis of structural fetal abnormalities revealed by ultrasound

Hillman

Carss

McMullan³

et al. 2014

Arch Dis Child Fetal Neonatal Ed

View full text Add to dashboard Cite

The genetic etiology of non-aneuploid fetal structural abnormalities is typically investigated by karyotyping and array-based detection of microscopically detectable rearrangements, and submicroscopic copy-number variants (CNVs), which collectively yield a pathogenic finding in up to 10% of cases. We propose that exome sequencing may substantially increase the identification of underlying etiologies. We performed exome sequencing on a cohort of 30 non-aneuploid fetuses and neonates (along with their parents) with diverse structural abnormalities first identified by prenatal ultrasound. We identified candidate pathogenic variants with a range of inheritance models, and evaluated these in the context of detailed phenotypic information. We identified 35 de novo single-nucleotide variants (SNVs), small indels, deletions or duplications, of which three (accounting for 10% of the cohort) are highly likely to be causative. These are de novo missense variants in FGFR3 and COL2A1, and a de novo 16.8 kb deletion that includes most of OFD1. In five further cases (17%) we identified de novo or inherited recessive or X-linked variants in plausible candidate genes, which require additional validation to determine pathogenicity. Our diagnostic yield of 10% is comparable to, and supplementary to, the diagnostic yield of existing microarray testing for large chromosomal rearrangements and targeted CNV detection. The de novo nature of these events could enable couples to be counseled as to their low recurrence risk. This study outlines the way for a substantial improvement in the diagnostic yield of prenatal genetic abnormalities through the application of next-generation sequencing.

show abstract

REREa/Atrophin‐2 interacts with histone deacetylase and Fgf8 signaling to regulate multiple processes of zebrafish development

Cited by 49 publications

References 58 publications

Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation

Histone deacetylase HDAC1/HDAC2-controlled embryonic development and cell differentiation

Atrophin Proteins Interact with the Fat1 Cadherin and Regulate Migration and Orientation in Vascular Smooth Muscle Cells

2.3 Exome sequencing improves genetic diagnosis of structural fetal abnormalities revealed by ultrasound

Contact Info

Product

Resources

About