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@ARTICLE{Fontebasso:120027,
author = {A. M. Fontebasso and S. Papillon-Cavanagh and J.
Schwartzentruber and H. Nikbakht and N. Gerges and P.-O.
Fiset and D. Bechet and D. Faury and N. De Jay and L. A.
Ramkissoon and A. Corcoran and D. Jones$^*$ and D. Sturm$^*$
and P. Johann$^*$ and T. Tomita and S. Goldman and M. Nagib
and A. Bendel and L. Goumnerova and D. C. Bowers and J. R.
Leonard and J. B. Rubin and T. Alden and S. Browd and J. R.
Geyer and S. Leary and G. Jallo and K. Cohen and N. Gupta
and M. D. Prados and A.-S. Carret and B. Ellezam and L.
Crevier and A. Klekner and L. Bognar and P. Hauser and M.
Garami and J. Myseros and Z. Dong and P. M. Siegel and H.
Malkin and A. H. Ligon and S. Albrecht and S. Pfister$^*$
and K. L. Ligon and J. Majewski and N. Jabado and M. W.
Kieran},
title = {{R}ecurrent somatic mutations in {ACVR}1 in pediatric
midline high-grade astrocytoma.},
journal = {Nature genetics},
volume = {46},
number = {5},
issn = {1546-1718},
address = {New York, NY},
publisher = {Nature America},
reportid = {DKFZ-2017-00615},
pages = {462 - 466},
year = {2014},
abstract = {Pediatric midline high-grade astrocytomas (mHGAs) are
incurable with few treatment targets identified. Most tumors
harbor mutations encoding p.Lys27Met in histone H3 variants.
In 40 treatment-naive mHGAs, 39 analyzed by whole-exome
sequencing, we find additional somatic mutations specific to
tumor location. Gain-of-function mutations in ACVR1 occur in
tumors of the pons in conjunction with histone H3.1
p.Lys27Met substitution, whereas FGFR1 mutations or fusions
occur in thalamic tumors associated with histone H3.3
p.Lys27Met substitution. Hyperactivation of the bone
morphogenetic protein (BMP)-ACVR1 developmental pathway in
mHGAs harboring ACVR1 mutations led to increased levels of
phosphorylated SMAD1, SMAD5 and SMAD8 and upregulation of
BMP downstream early-response genes in tumor cells. Global
DNA methylation profiles were significantly associated with
the p.Lys27Met alteration, regardless of the mutant histone
H3 variant and irrespective of tumor location, supporting
the role of this substitution in driving the epigenetic
phenotype. This work considerably expands the number of
potential treatment targets and further justifies
pretreatment biopsy in pediatric mHGA as a means to orient
therapeutic efforts in this disease.},
keywords = {Bone Morphogenetic Proteins (NLM Chemicals) / Smad Proteins
(NLM Chemicals) / ACVR1 protein, human (NLM Chemicals) /
Activin Receptors, Type I (NLM Chemicals)},
cin = {B062},
ddc = {570},
cid = {I:(DE-He78)B062-20160331},
pnm = {312 - Functional and structural genomics (POF3-312)},
pid = {G:(DE-HGF)POF3-312},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:24705250},
pmc = {pmc:PMC4282994},
doi = {10.1038/ng.2950},
url = {https://inrepo02.dkfz.de/record/120027},
}