Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmitoylation and signaling.

The Hedgehog (Hh) family of secreted proteins act as morphogens to control embryonic patterning and development in a variety of organ systems. Post-translational covalent attachment of cholesterol and palmitate to Hh proteins are critical for multimerization and long range signaling potency. However...

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Main Authors: Patrick Callier, Pierre Calvel, Armine Matevossian, Periklis Makrythanasis, Pascal Bernard, Hiroshi Kurosaka, Anne Vannier, Christel Thauvin-Robinet, Christelle Borel, Séverine Mazaud-Guittot, Antoine Rolland, Christèle Desdoits-Lethimonier, Michel Guipponi, Céline Zimmermann, Isabelle Stévant, Françoise Kuhne, Béatrice Conne, Federico Santoni, Sandy Lambert, Frederic Huet, Francine Mugneret, Jadwiga Jaruzelska, Laurence Faivre, Dagmar Wilhelm, Bernard Jégou, Paul A Trainor, Marilyn D Resh, Stylianos E Antonarakis, Serge Nef
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-05-01
Series:PLoS Genetics
Online Access:https://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1004340&type=printable
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author Patrick Callier
Pierre Calvel
Armine Matevossian
Periklis Makrythanasis
Pascal Bernard
Hiroshi Kurosaka
Anne Vannier
Christel Thauvin-Robinet
Christelle Borel
Séverine Mazaud-Guittot
Antoine Rolland
Christèle Desdoits-Lethimonier
Michel Guipponi
Céline Zimmermann
Isabelle Stévant
Françoise Kuhne
Béatrice Conne
Federico Santoni
Sandy Lambert
Frederic Huet
Francine Mugneret
Jadwiga Jaruzelska
Laurence Faivre
Dagmar Wilhelm
Bernard Jégou
Paul A Trainor
Marilyn D Resh
Stylianos E Antonarakis
Serge Nef
author_facet Patrick Callier
Pierre Calvel
Armine Matevossian
Periklis Makrythanasis
Pascal Bernard
Hiroshi Kurosaka
Anne Vannier
Christel Thauvin-Robinet
Christelle Borel
Séverine Mazaud-Guittot
Antoine Rolland
Christèle Desdoits-Lethimonier
Michel Guipponi
Céline Zimmermann
Isabelle Stévant
Françoise Kuhne
Béatrice Conne
Federico Santoni
Sandy Lambert
Frederic Huet
Francine Mugneret
Jadwiga Jaruzelska
Laurence Faivre
Dagmar Wilhelm
Bernard Jégou
Paul A Trainor
Marilyn D Resh
Stylianos E Antonarakis
Serge Nef
author_sort Patrick Callier
collection DOAJ
description The Hedgehog (Hh) family of secreted proteins act as morphogens to control embryonic patterning and development in a variety of organ systems. Post-translational covalent attachment of cholesterol and palmitate to Hh proteins are critical for multimerization and long range signaling potency. However, the biological impact of lipid modifications on Hh ligand distribution and signal reception in humans remains unclear. In the present study, we report a unique case of autosomal recessive syndromic 46,XY Disorder of Sex Development (DSD) with testicular dysgenesis and chondrodysplasia resulting from a homozygous G287V missense mutation in the hedgehog acyl-transferase (HHAT) gene. This mutation occurred in the conserved membrane bound O-acyltransferase (MBOAT) domain and experimentally disrupted the ability of HHAT to palmitoylate Hh proteins such as DHH and SHH. Consistent with the patient phenotype, HHAT was found to be expressed in the somatic cells of both XX and XY gonads at the time of sex determination, and Hhat loss of function in mice recapitulates most of the testicular, skeletal, neuronal and growth defects observed in humans. In the developing testis, HHAT is not required for Sertoli cell commitment but plays a role in proper testis cord formation and the differentiation of fetal Leydig cells. Altogether, these results shed new light on the mechanisms of action of Hh proteins. Furthermore, they provide the first clinical evidence of the essential role played by lipid modification of Hh proteins in human testicular organogenesis and embryonic development.
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publishDate 2014-05-01
publisher Public Library of Science (PLoS)
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spelling doaj-art-639ab364e74943b08783e497d9a164d02025-08-20T03:00:29ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042014-05-01105e100434010.1371/journal.pgen.1004340Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmitoylation and signaling.Patrick CallierPierre CalvelArmine MatevossianPeriklis MakrythanasisPascal BernardHiroshi KurosakaAnne VannierChristel Thauvin-RobinetChristelle BorelSéverine Mazaud-GuittotAntoine RollandChristèle Desdoits-LethimonierMichel GuipponiCéline ZimmermannIsabelle StévantFrançoise KuhneBéatrice ConneFederico SantoniSandy LambertFrederic HuetFrancine MugneretJadwiga JaruzelskaLaurence FaivreDagmar WilhelmBernard JégouPaul A TrainorMarilyn D ReshStylianos E AntonarakisSerge NefThe Hedgehog (Hh) family of secreted proteins act as morphogens to control embryonic patterning and development in a variety of organ systems. Post-translational covalent attachment of cholesterol and palmitate to Hh proteins are critical for multimerization and long range signaling potency. However, the biological impact of lipid modifications on Hh ligand distribution and signal reception in humans remains unclear. In the present study, we report a unique case of autosomal recessive syndromic 46,XY Disorder of Sex Development (DSD) with testicular dysgenesis and chondrodysplasia resulting from a homozygous G287V missense mutation in the hedgehog acyl-transferase (HHAT) gene. This mutation occurred in the conserved membrane bound O-acyltransferase (MBOAT) domain and experimentally disrupted the ability of HHAT to palmitoylate Hh proteins such as DHH and SHH. Consistent with the patient phenotype, HHAT was found to be expressed in the somatic cells of both XX and XY gonads at the time of sex determination, and Hhat loss of function in mice recapitulates most of the testicular, skeletal, neuronal and growth defects observed in humans. In the developing testis, HHAT is not required for Sertoli cell commitment but plays a role in proper testis cord formation and the differentiation of fetal Leydig cells. Altogether, these results shed new light on the mechanisms of action of Hh proteins. Furthermore, they provide the first clinical evidence of the essential role played by lipid modification of Hh proteins in human testicular organogenesis and embryonic development.https://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1004340&type=printable
spellingShingle Patrick Callier
Pierre Calvel
Armine Matevossian
Periklis Makrythanasis
Pascal Bernard
Hiroshi Kurosaka
Anne Vannier
Christel Thauvin-Robinet
Christelle Borel
Séverine Mazaud-Guittot
Antoine Rolland
Christèle Desdoits-Lethimonier
Michel Guipponi
Céline Zimmermann
Isabelle Stévant
Françoise Kuhne
Béatrice Conne
Federico Santoni
Sandy Lambert
Frederic Huet
Francine Mugneret
Jadwiga Jaruzelska
Laurence Faivre
Dagmar Wilhelm
Bernard Jégou
Paul A Trainor
Marilyn D Resh
Stylianos E Antonarakis
Serge Nef
Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmitoylation and signaling.
PLoS Genetics
title Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmitoylation and signaling.
title_full Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmitoylation and signaling.
title_fullStr Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmitoylation and signaling.
title_full_unstemmed Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmitoylation and signaling.
title_short Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmitoylation and signaling.
title_sort loss of function mutation in the palmitoyl transferase hhat leads to syndromic 46 xy disorder of sex development by impeding hedgehog protein palmitoylation and signaling
url https://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1004340&type=printable
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