Mammalian achaete-scute homolog 1 is required for the early development of olfactory and autonomic neurons

Guillemot, François; Lo, L.; Johnson, Jane E.; Auerbach, Anna B.; Anderson, David J.; Joyner, Alexandra L.

doi:10.1016/0092-8674(93)90381-y

Cited by 971 publications

(718 citation statements)

References 67 publications

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“…ASCL proteins dimerize through their helix-loop-helix domains, which permits their basic domains to bind canonical E-box elements and thereby control transcription (Massari and Murre, 2000). ascl1 (Johnson et al, 1990) and ascl2 (Johnson et al, 1990;Guillemot et al, 1994) function as lineagespecific transcription factors essential for development of the neurectoderm (Guillemot et al, 1993) and trophectoderm (Guillemot et al, 1994(Guillemot et al, , 1995, respectively. ascl1 is frequently expressed in human neoplasia with neuroendocrine features (Westerman et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Achaete-scute like 2 (ascl2) is a target of Wnt signalling and is upregulated in intestinal neoplasia

Jubb

Chalasani²,

Frantz³

et al. 2006

Oncogene

119

112

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Achaete-scute like (ASCL)2 is a basic helix-loop-helix transcription factor essential for the maintenance of proliferating trophoblasts during placental development. Using oligonucleotide microarrays we identified ascl2 as a gene significantly upregulated in colorectal adenocarcinomas (n ¼ 36 cancers, n ¼ 16 normals; 15-fold, Po0.0001). This finding was confirmed by quantitative reverse transcriptase (RT)-PCR on large intestinal cancers (n ¼ 29 cancers, n ¼ 16 normals; 10-fold, Po0.0001).In situ hybridization for ascl2 demonstrated expression at the base of small and large intestinal crypts (n ¼ 304), but in no other normal tissues excepting placenta. By in situ hybridization, 52-71% of colorectal adenomas (n ¼ 187), 50-73% of large (n ¼ 327) and 33-64% of small intestinal adenocarcinomas (n ¼ 124) were positive for ascl2 expression. Upregulation of murine ascl2 was also observed using oligonucleotide microarrays, quantitative RT-PCR and in situ hybridization on apc min/ þ and apc 1638N/ þ smad4 À/ þ tumours. Tumour cell lines stably transfected with LEF1 DN or APC2, or transiently transfected with short-interfering RNA (siRNA) against b-catenin showed a significant downregulation of ascl2. Colocalization of ascl2 with nuclear b-catenin was observed in 73 small intestinal adenocarcinomas (P ¼ 0.0008) and apc min/ þ tumours. Preliminary in vitro data suggest ascl2 may promote progression through the G2/M cell cycle checkpoint. In summary, ascl2 is a putative regulator of proliferation that is overexpressed in intestinal neoplasia.

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Section: Introductionmentioning

confidence: 99%

Achaete-scute like 2 (ascl2) is a target of Wnt signalling and is upregulated in intestinal neoplasia

Jubb

Chalasani²,

Frantz³

et al. 2006

Oncogene

119

112

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“…These ubiquitous E2A proteins form active heterodimers with tissuespecific bHLH proteins, which then bind to DNA and activate the transcription of target genes. Tissue-specific bHLH proteins associated with E2A proteins include the MyoD family involved in skeletal muscle differentiation (Weintraub, 1993), the achaete-scute family involved in neuronal differentiation (Guillemot et al, 1993), and SCL/TAL which is involved in hematopoiesis (Hsu et al, 1991). The E2A proteins are also required for lymphocyte development, and have also been implicated in cell growth, apoptosis and lymphomagenesis (Bain et al, 1994;Peverali et al, 1994;Yan et al, 1997;Quong et al, 2002;Lazorchak et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

E2A protein degradation by the ubiquitin-proteasome system is stage-dependent during muscle differentiation

et al. 2006

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The E2A proteins are basic helix-loop-helix transcription factors that regulate proliferation and differentiation in many cell types. In muscle cells, the E2A proteins form heterodimers with muscle regulatory factors such as MyoD, which then bind to DNA and regulate the transcription of target genes essential for muscle differentiation. We now demonstrate that E2A proteins are primarily localized in the nucleus in both C2C12 myoblasts and myotubes, and are degraded by the ubiquitin proteasome system evidenced by stabilization following treatment with the proteasome inhibitor, MG132. During the differentiation from myoblast to myotube, the cellular abundance of E2A proteins is relatively unaltered, despite significant changes (each B5-fold) in the relative rates of protein synthesis and protein degradation via the ubiquitin-proteasome system. The rate of ubiquitin-proteasome-mediated E2A protein degradation depends on the myogenic differentiation state (t½B2 h in proliferating myoblasts versus t½>10 h in differentiated myotubes), and is also associated with cell cycle in non-muscle cells. Our findings reveal an important role for both translational and post-translational regulatory mechanisms in mediating the complex program of muscle differentiation determined by the E2A proteins.

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“…However, Mash1 is essential for the differentiation of neuroendocrine cells in the lung, the adrenal gland, the thyroid, and is thus an important factor regulating endocrine development in another context (Ball, 2004, Huber et al, 2002, Lanigan et al, 1998. Interestingly, differentiation and survival of the mouse olfactory epithelium depends on Mash1 function comparable to that of Ascl1a in zebrafish pituitary development (Guillemot et al, 1993). Since olfactory and AH precursors originate from closely juxtaposed positions within the anterior preplacodal region (see above), the related pituitary and nose phenotype might point at a common evolutionary origin of the affected cell types (Gorbman, 1995).…”

mentioning

confidence: 99%

How to make a teleost adenohypophysis: Molecular pathways of pituitary development in zebrafish

Pogoda

Hammerschmidt

2009

Molecular and Cellular Endocrinology

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Please cite this article as: Pogoda, H.-M., Hammerschmidt, M., How to make a Teleost Adenohypophysis: Molecular Pathways of Pituitary development in Zebrafish, Molecular and Cellular Endocrinology (2008), doi:10.1016/j.mce.2009 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. In the past years, the zebrafish has emerged as a powerful tool to elucidate the genetic networks controlling vertebrate development, behavior and disease. Based on mutants isolated in forward genetic screens and on gene knock-downs using morpholino oligonucleotide (oligo) antisense technology, our current understanding of the molecular machinery driving adenohypophyseal ontogeny could be considerably improved. In addition, comparative analyses have shed further light onto the evolution of this rather recently invented organ. The goal of this review is to summarize current knowledge of the genetic and molecular control of zebrafish pituitary development, with special focus on most recent findings, including some thus far unpublished data from our own laboratory on the transcription factor Six1. In addition, zebrafish data will be discussed in comparison with current understanding of adenohypophysis development in mouse.

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Mammalian achaete-scute homolog 1 is required for the early development of olfactory and autonomic neurons

Cited by 971 publications

References 67 publications

Achaete-scute like 2 (ascl2) is a target of Wnt signalling and is upregulated in intestinal neoplasia

Achaete-scute like 2 (ascl2) is a target of Wnt signalling and is upregulated in intestinal neoplasia

E2A protein degradation by the ubiquitin-proteasome system is stage-dependent during muscle differentiation

How to make a teleost adenohypophysis: Molecular pathways of pituitary development in zebrafish

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