CLK2 inhibition ameliorates autistic features associated with SHANK3 deficiency

Science

Volumn 351, Issue 6278, 2016, Pages 1199-1203

  Bidinosti, Michael ^a   Botta, Paolo ^b   Kröttner, Sebastian ^b   Proenca, Catia C ^a   Stoehr, Natacha ^a   Bernhard, Mario ^a   Fruh, Isabelle ^a   Mueller, Matthias ^a   Bonenfant, Debora ^a   Voshol, Hans ^a   Carbone, Walter ^a   Neal, Sarah J ^c   McTighe, Stephanie M ^c   Roma, Guglielmo ^a   Dolmetsch, Ricardo E ^c   Porter, Jeffrey A ^a   Caroni, Pico ^b   Bouwmeester, Tewis ^a   Löthi, Andreas ^b   Galimberti, Ivan ^a  

^a NOVARTIS PHARMA AG   (Switzerland)

^b FRIEDRICH MIESCHER INSTITUTE FOR BIOMEDICAL RESEARCH   (Switzerland)

^c NOVARTIS INSTITUTES FOR BIOMEDICAL RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CDC2 LIKE KINASE 2; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN KINASE B; PROTEIN SH3; SERINE; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS 3; SOMATOMEDIN C; THREONINE; UNCLASSIFIED DRUG; CLK DUAL-SPECIFICITY KINASES; INSULIN-LIKE GROWTH FACTOR-1, MOUSE; MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1; MULTIPROTEIN COMPLEX; NERVE PROTEIN; PHOSPHOPROTEIN PHOSPHATASE 2; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE; SHANK3 PROTEIN, MOUSE; TARGET OF RAPAMYCIN KINASE;

BIOCHEMISTRY; ENZYME ACTIVITY; GENE EXPRESSION; INHIBITION; MENTAL HEALTH; PHOSPHATASE; PROTEIN; PROTEOMICS; RODENT;

ANIMAL CELL; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; AUTISM; CONTROLLED STUDY; DOWN REGULATION; ENZYME ACTIVATION; ENZYME INHIBITION; ENZYME PHOSPHORYLATION; HUMAN; HUMAN CELL; MOLECULAR PATHOLOGY; MOUSE; NERVE CELL; NONHUMAN; PHELAN-MCDERMID SYNDROME; PRIORITY JOURNAL; PROTEOMICS; RAT; SIGNAL TRANSDUCTION; UBIQUITINATION; AMINO ACID SEQUENCE; ANIMAL; ANTAGONISTS AND INHIBITORS; AUTISM SPECTRUM DISORDER; CHROMOSOME 22; CHROMOSOME DELETION; CHROMOSOME DISORDER; DISEASE MODEL; ENZYMOLOGY; GENE SILENCING; GENETICS; METABOLISM; MOLECULAR GENETICS; PHOSPHORYLATION;

MAMMALIA;

AMINO ACID SEQUENCE; ANIMALS; AUTISM SPECTRUM DISORDER; CHROMOSOME DELETION; CHROMOSOME DISORDERS; CHROMOSOMES, HUMAN, PAIR 22; DISEASE MODELS, ANIMAL; DOWN-REGULATION; GENE KNOCKDOWN TECHNIQUES; HUMANS; INSULIN-LIKE GROWTH FACTOR I; MICE; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; NERVE TISSUE PROTEINS; NEURONS; PHOSPHORYLATION; PROTEIN PHOSPHATASE 2; PROTEIN-SERINE-THREONINE KINASES; PROTEIN-TYROSINE KINASES; PROTEOMICS; PROTO-ONCOGENE PROTEINS C-AKT; RATS; SIGNAL TRANSDUCTION; TOR SERINE-THREONINE KINASES;

EID: 84960871327     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aad5487     Document Type: Article

References (27)

1. K. Phelan, H. E. McDermid, Molecular Syndromology 2, 186-201 (2012).
2. C. Redin et al., J. Med. Genet. 51, 724-736 (2014).
3. J. Gauthier et al., Proc. Natl. Acad. Sci. U.S.A. 107, 7863-7868 (2010).
4. C. M. Durand et al., Nat. Genet. 39, 25-27 (2007).
5. O. Bozdagi et al., Molecular Autism 1, 15 (2010).
6. J. Peça et al., Nature 472, 437-442 (2011).
7. X. Wang et al., Hum. Mol. Genet. 20, 3093-3108 (2011).
8. M. Kouser et al., J. Neurosci. 33, 18448-18468 (2013).
9. M. Yang et al., J. Neurosci. 32, 6525-6541 (2012).
10. L. J. Duffney et al., Cell Reports 11, 1400-1413 (2015).
11. C. Verpelli et al., J. Biol. Chem. 286, 34839-34850 (2011).
12. A. Shcheglovitov et al., Nature 503, 267-271 (2013).
13. Y. H. Jiang, M. D. Ehlers, Neuron 78, 8-27 (2013).
14. G. Roussignol et al., J. Neurosci. 25, 3560-3570 (2005).
15. K. Han et al., Nature 503, 72-77 (2013).
16. A. Kolevzon et al., Molecular Autism 5, 54 (2014).
17. O. Bozdagi, T. Tavassoli, J. D. Buxbaum, Molecular Autism 4, 9 (2013).
18. S. Padmanabhan et al., Cell 136, 939-951 (2009).
19. J. T. Rodgers, R. O. Vogel, P. Puigserver, Mol. Cell 41, 471-479 (2011).
20. C. M. Gower et al., ACS Chem. Biol. 11, 121-131 (2016).
21. A. Goffin, L. H. Hoefsloot, E. Bosgoed, A. Swillen, J. P. Fryns, Am. J. Med. Genet. 105, 521-524 (2001).
22. S. L. Smalley, P. E. Tanguay, M. Smith, G. Gutierrez, J. Autism Dev. Disord. 22, 339-355 (1992).
23. B. McCright, D. M. Virshup, J. Biol. Chem. 270, 26123-26128 (1995).
24. J. T. Rodgers, W. Haas, S. P. Gygi, P. Puigserver, Cell Metab. 11, 23-34 (2010).
25. H. Jo et al., Proc. Natl. Acad. Sci. U.S.A. 109, 10581-10586 (2012).
26. S. Ricciardi et al., Hum. Mol. Genet. 20, 1182-1196 (2011).
27. C. Cao et al., PLOS Biol. 11, e1001478 (2013).