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Human Molecular Genetics, 2000, Vol. 9, No. 11 1681-1690
© 2000 Oxford University Press

DSCR1, overexpressed in Down syndrome, is an inhibitor of calcineurin-mediated signaling pathways

Juan J. Fuentes, Lali Genescà, Tami J. Kingsbury1, Kyle W. Cunningham1, Mercè Pérez-Riba, Xavier Estivill+ and Susana de la Luna

Down Syndrome Research Group, Medical and Molecular Genetics Center, IRO, Hospital Duran i Reynals, Avia de Castelldefels Km 2.7, 08907-L’Hospitalet de Llobregat, Barcelona, Spain and 1Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA

Down syndrome is one of the major causes of mental retardation and congenital heart malformations. Other common clinical features of Down syndrome include gastrointestinal anomalies, immune system defects and Alzheimer’s disease pathological and neurochemical changes. The most likely consequence of the presence of three copies of chromosome 21 is the overexpression of its resident genes, a fact which must underlie the pathogenesis of the abnormalities that occur in Down syndrome. Here we show that DSCR1, the product of a chromosome 21 gene highly expressed in brain, heart and skeletal muscle, is overexpressed in the brain of Down syndrome fetuses, and interacts physically and functionally with calcineurin A, the catalytic subunit of the Ca2+/calmodulin-dependent protein phosphatase PP2B. The DSCR1 binding region in calcineurin A is located in the linker region between the calcineurin A catalytic domain and the calcineurin B binding domain, outside of other functional domains previously defined in calcineurin A. DSCR1 belongs to a family of evolutionarily conserved proteins with three members in humans: DSCR1, ZAKI-4 and DSCR1L2. We further demonstrate that overexpression of DSCR1 and ZAKI-4 inhibits calcineurin-dependent gene transcription through the inhibition of NF-AT translocation to the nucleus. Together, these results suggest that members of this newly described family of human proteins are endogenous regulators of calcineurin-mediated signaling pathways and as such, they may be involved in many physiological processes.

+ To whom correspondence should be addressed. Tel: +34 93 2607775; Fax: +34 93 2607776; Email: estivill@iro.es


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Targeted inhibition of calcineurin attenuates cardiac hypertrophy invivo
PNAS, March 13, 2001; 98(6): 3322 - 3327.
[Abstract] [Full Text] [PDF]

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 Proc. Natl. Acad. Sci. USAHome page
B. A. Rothermel, T. A. McKinsey, R. B. Vega, R. L. Nicol, P. Mammen, J. Yang, C. L. Antos, J. M. Shelton, R. Bassel-Duby, E. N. Olson, et al.
Myocyte-enriched calcineurin-interacting protein, MCIP1, inhibits cardiac hypertrophy in vivo
PNAS, March 13, 2001; 98(6): 3328 - 3333.
[Abstract] [Full Text] [PDF]

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 Circ. Res.Home page
J. Yang, B. Rothermel, R. B. Vega, N. Frey, T. A. McKinsey, E. N. Olson, R. Bassel-Duby, and R. S. Williams
Independent Signals Control Expression of the Calcineurin Inhibitory Proteins MCIP1 and MCIP2 in Striated Muscles
Circ. Res., December 8, 2000; 87 (12): e61 - e68.
[Abstract] [Full Text] [PDF]

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 Circ. Res.Home page
J. D. Molkentin
Calcineurin and Beyond : Cardiac Hypertrophic Signaling
Circ. Res., October 27, 2000; 87(9): 731 - 738.
[Abstract] [Full Text] [PDF]

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 J. Biol. Chem.Home page
G. R. Crabtree
Calcium, Calcineurin, and the Control of Transcription
J. Biol. Chem., January 19, 2001; 276(4): 2313 - 2316.
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 Proc. Natl. Acad. Sci. USAHome page
O. F. Bueno, B. J. Wilkins, K. M. Tymitz, B. J. Glascock, T. F. Kimball, J. N. Lorenz, and J. D. Molkentin
Impaired cardiac hypertrophic response in Calcineurin Abeta -deficient mice
PNAS, April 2, 2002; 99(7): 4586 - 4591.
[Abstract] [Full Text] [PDF]


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