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Mutations in PIK3C2A cause syndromic short stature, skeletal abnormalities, and cataracts associated with ciliary dysfunction.
Tiosano, Dov; Baris, Hagit N; Chen, Anlu; Hitzert, Marrit M; Schueler, Markus; Gulluni, Federico; Wiesener, Antje; Bergua, Antonio; Mory, Adi; Copeland, Brett; Gleeson, Joseph G; Rump, Patrick; van Meer, Hester; Sival, Deborah A; Haucke, Volker; Kriwinsky, Josh; Knaup, Karl X; Reis, André; Hauer, Nadine N; Hirsch, Emilio; Roepman, Ronald; Pfundt, Rolph; Thiel, Christian T; Wiesener, Michael S; Aslanyan, Mariam G; Buchner, David A.
Afiliação
  • Tiosano D; Division of Pediatric Endocrinology, Ruth Children's Hospital, Rambam Medical Center, Haifa, Israel.
  • Baris HN; Rappaport Family Faculty of Medicine, Technion-Israel Institute of Technology, Haifa, Israel.
  • Chen A; Rappaport Family Faculty of Medicine, Technion-Israel Institute of Technology, Haifa, Israel.
  • Hitzert MM; The Genetics Institute, Rambam Health Care Campus, Haifa, Israel.
  • Schueler M; Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio, United States of America.
  • Gulluni F; Department of Genetics, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
  • Wiesener A; Department of Nephrology and Hypertension, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
  • Bergua A; Department of Molecular Biotechnology and Health Sciences, Molecular Biotechnology Center, University of Turin, Torino, Italy.
  • Mory A; Institute of Human Genetics, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
  • Copeland B; Department of Ophthalmology, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
  • Gleeson JG; The Genetics Institute, Rambam Health Care Campus, Haifa, Israel.
  • Rump P; Laboratory of Pediatric Brain Diseases, Rockefeller University, New York, New York, United States of America.
  • van Meer H; Laboratory of Pediatric Brain Diseases, Rockefeller University, New York, New York, United States of America.
  • Sival DA; Department of Neurosciences, University of California, San Diego, La Jolla, California, United States of America.
  • Haucke V; Department of Genetics, University of Groningen, University Medical Center Groningen, Groningen, The Netherlands.
  • Kriwinsky J; Department of Pediatrics, Beatrix Children's Hospital, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands.
  • Knaup KX; Department of Pediatrics, Beatrix Children's Hospital, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands.
  • Reis A; Leibniz-Institut für Molekulare Pharmakologie, Berlin Faculty of Biology, Chemistry, and Pharmacy, Freie Universität Berlin, Berlin, Germany.
  • Hauer NN; Department of Genetics and Genome Sciences, Case Western Reserve University, Cleveland, Ohio, United States of America.
  • Hirsch E; Department of Nephrology and Hypertension, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
  • Roepman R; Institute of Human Genetics, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
  • Pfundt R; Institute of Human Genetics, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
  • Thiel CT; Department of Molecular Biotechnology and Health Sciences, Molecular Biotechnology Center, University of Turin, Torino, Italy.
  • Wiesener MS; Department of Human Genetics, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen, The Netherlands.
  • Aslanyan MG; Department of Human Genetics, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen, The Netherlands.
  • Buchner DA; Institute of Human Genetics, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
PLoS Genet ; 15(4): e1008088, 2019 04.
Article em En | MEDLINE | ID: mdl-31034465
PIK3C2A is a class II member of the phosphoinositide 3-kinase (PI3K) family that catalyzes the phosphorylation of phosphatidylinositol (PI) into PI(3)P and the phosphorylation of PI(4)P into PI(3,4)P2. At the cellular level, PIK3C2A is critical for the formation of cilia and for receptor mediated endocytosis, among other biological functions. We identified homozygous loss-of-function mutations in PIK3C2A in children from three independent consanguineous families with short stature, coarse facial features, cataracts with secondary glaucoma, multiple skeletal abnormalities, neurological manifestations, among other findings. Cellular studies of patient-derived fibroblasts found that they lacked PIK3C2A protein, had impaired cilia formation and function, and demonstrated reduced proliferative capacity. Collectively, the genetic and molecular data implicate mutations in PIK3C2A in a new Mendelian disorder of PI metabolism, thereby shedding light on the critical role of a class II PI3K in growth, vision, skeletal formation and neurological development. In particular, the considerable phenotypic overlap, yet distinct features, between this syndrome and Lowe's syndrome, which is caused by mutations in the PI-5-phosphatase OCRL, highlight the key role of PI metabolizing enzymes in specific developmental processes and demonstrate the unique non-redundant functions of each enzyme. This discovery expands what is known about disorders of PI metabolism and helps unravel the role of PIK3C2A and class II PI3Ks in health and disease.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doenças do Desenvolvimento Ósseo / Catarata / Transtornos da Motilidade Ciliar / Fosfatidilinositol 3-Quinases / Nanismo / Mutação Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doenças do Desenvolvimento Ósseo / Catarata / Transtornos da Motilidade Ciliar / Fosfatidilinositol 3-Quinases / Nanismo / Mutação Idioma: En Ano de publicação: 2019 Tipo de documento: Article