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  THE DOWN SYNDROME CANDIDATE DUAL-SPECIFICITY TYROSINE PHOSPHORYLATION-REGULATED KINASE 1A PHOSPHORYLATES THE NEURODEGENERATION-RELATED SEPTIN 4

Sitz, J. H., Baumgärtel, K., Hämmerle, B., Papadopoulos, C., Hekerman, P., Tejedor, F. J., et al. (2008). THE DOWN SYNDROME CANDIDATE DUAL-SPECIFICITY TYROSINE PHOSPHORYLATION-REGULATED KINASE 1A PHOSPHORYLATES THE NEURODEGENERATION-RELATED SEPTIN 4. Neuroscience, 157(3), 596-605.

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 Urheber:
Sitz, J. H.1, Autor           
Baumgärtel, K., Autor
Hämmerle, B., Autor
Papadopoulos, C., Autor
Hekerman, P., Autor
Tejedor, F. J., Autor
Becker, W., Autor
Lutz, B.1, Autor           
Affiliations:
1Max Planck Institute of Psychiatry, Max Planck Society, ou_1607137              

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Schlagwörter: trisomy 21; scaffold; protein interaction; harmine; DYRK1A; SEPT4
 Zusammenfassung: The dual-specific kinase DYRK1A (dual-specificity tyrosine phosphorylation-regulated kinase 1A) is the mammalian orthologue of the Drosophila minibrain (MNB) protein kinase and executes diverse roles in neuronal development and adult brain physiology. DYRK1A is overexpressed in Down syndrome (DS) and has recently been implicated in several neurodegenerative diseases. In an attempt to elucidate the molecular basis of its involvement in cognitive and neurodegeneration processes, we searched for novel proteins interacting with the kinase domain of DYRK1A in the adult mouse brain and identified septin 4 (SEPT4, also known as Pnutl2/CDCrel-2). SEPT4 is a member of the group III septin family of guanosine triphosphate hydrolases (GTPases), which has previously been found in neurofibrillary tangles of Alzheimer disease brains and in a-synuclein-positive cytoplasmic inclusions in Parkinson disease brains. In transfected mammalian cells, DYRK1A specifically interacts with and phosphorylates SEPT4. Phosphorylation of SEPT4 by DYRK1A was inhibited by harmine, which has recently been identified as the most specific inhibitor of DYRK1A. In support of a physiological relation in the brain, we found that Dyrk1A and Sept4 are coexpressed and co-localized in neocortical neurons. These findings suggest that SEPT4 is a substrate of DYRK1A kinase and thus provide a possible link for the involvement of DYRK1A in neurodegenerative processes and in DS neuropathologies. (C) 2008 IBRO. Published by Elsevier Ltd. All rights reserved.

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Sprache(n): eng - English
 Datum: 2008-12-02
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 396559
ISI: 000261464800011
 Art des Abschluß: -

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Titel: Neuroscience
Genre der Quelle: Zeitschrift
 Urheber:
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 157 (3) Artikelnummer: - Start- / Endseite: 596 - 605 Identifikator: ISSN: 0306-4522