Mnb/Dyrk1a Phosphorylation Regulates the Interactions of Synaptojanin 1 with Endocytic Accessory Proteins.
From: Molecular Biology Department, NYS Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA.
Biochemical and biophysical research communications
- Publish Date: Dec 2006
- ISSN: 0006-291X
- Volume: 351
- Issue: 4
- Pages: 1060-5
- Medium: Print
- Language: English
- Citation (JAMA): Adayev Tatyana, Chen-Hwang Mo-Chou, Murakami Noriko, et al. Mnb/Dyrk1a Phosphorylation Regulates the Interactions of Synaptojanin 1 with Endocytic Accessory Proteins.. Biochem. Biophys. Res. Commun. Dec 2006;351:1060-5
Abstract
MNB/DYRK1A is a proline-directed serine/threonine kinase implicated in Down syndrome (DS). In an earlier screening, two proteins from adult rat brain, one 100kDa and the other 140 kDa, were found to be prominently phosphorylated by the kinase. The 100-kDa protein was previously characterized as an isoform of dynamin 1. In this study, we identified the 140-kDa protein as synaptojanin 1 (SJ1). MNB/DYRK1A phosphorylates SJ1 at multiple sites and produces complex behaviors in binding to amphiphysin 1 and intersectin 1 (ITSN1). However, the phosphorylation has little effect on the phosphatidylinositol phosphatase activity of SJ1. These results suggest that MNB/DYRK1A is involved in regulating the recruitment activity but not the phosphatase activity of SJ1. Our findings may be especially important in the etiology of DS because MNB/DYRK1A, SJ1, and ITSN1 are all located at or near the region of human chromosome 21, which is postulated to be involved in the disease.
Mesh Headings (Keywords): Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Animals, Cells, Cultured, Endocytosis, Humans, Mice, Molecular Sequence Data, Nerve Tissue Proteins, Phosphoric Monoester Hydrolases, Phosphorylation, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, Rats, Substrate Specificity
Check for Full Text / PubMed Unique Identifier (PMID): 17097615
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