Dual Specificity Tyrosine-(Y)-Phosphorylation-Regulated Kinase (DYRK)

Sino Biological provides a comprehensive set of tools for Dual specificity tyrosine-(Y)-phosphorylation-regulated kinases (DYRK) related studies, including proteins, antibodies (rabbit mAbs, mouse mAbs, and rabbit pAbs), ELISA kits, and ORF cDNA clones. Dual specificity tyrosine-(Y)-phosphorylation-regulated kinases (DYRK) are dual-specificity protein kinases that catalyze autophosphorylation on serine/threonine and tyrosine residues. Kinases of DYRK family play key roles in the regulation of cell differentiation, proliferation, and survival. Members of DYRK family kinases share structural similarity, however, differ in their substrate specificity, suggesting their involvement in different cellular functions.

Dual Specificity Tyrosine-(Y)-Phosphorylation-Regulated Kinase (DYRK) Products

• DYRK2
• DYRK3
• DYRK4

Dual Specificity Tyrosine-(Y)-Phosphorylation-Regulated Kinase (DYRK) Background

Dual specificity tyrosine-(Y)-phosphorylation-regulated kinases (DYRK) are dual-specificity protein kinases that catalyze autophosphorylation on serine/threonine and tyrosine residues. Kinases of DYRK family play key roles in the regulation of cell differentiation, proliferation, and survival. Members of DYRK family kinases share structural similarity, however, differ in their substrate specificity, suggesting their involvement in different cellular functions.

Dual specificity tyrosine-(Y)-phosphorylation-regulated kinase 1A (DYRK1A) is the mammalian orthologue of the Drosophila minibrain (MNB) protein kinaseis. It is localized in the Down syndrome critical region of chromosome 21, and is considered to be a strong candidate gene for learning defects associated with Down syndrome. DYRK1A executes diverse roles in neuronal development and adult brain physiology, and has recently been implicated in several neurodegenerative diseases.

Dual specificity tyrosine-(Y)-phosphorylation-regulated kinase 2 (DYRK2) has demonstrated tyrosine autophosphorylation and catalyzed phosphorylation of histones H3 and H2B in vitro. Miller CT, et al. (2003) reported DYRK2 mRNA overexpression (>2.5-fold of normal mean) in lung adenocarcinomas in an assay using oligonucleotide microarrays. It is the first to report amplification and overexpression of DYRK2 in any human cancer.

Dual specificity tyrosine-(Y)-phosphorylation-regulated kinase 3 (DYRK3) has also been shown to autophosphorylate on tyrosine residue and catalyze phosphorylation of histones H3 and H2B in vitro. Alternatively spliced transcript variants encoding different isoforms have been identified.

Dual specificity tyrosine-(Y)-phosphorylation-regulated kinase 4 (DYRK4) is the least studied DYRK family members. Splice variants of DYRK4 have been identified, which differ in their subcellular localization and catalytic activity.

Dual Specificity Tyrosine-(Y)-Phosphorylation-Regulated Kinase (DYRK) Related Studies

1. Miller CT, et al. (2003) Amplification and overexpression of the dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 2 (DYRK2) gene in esophageal and lung adenocarcinomas. Cancer Res. 63(14):4136-43.
2. Murakami N, et al. (2006) Phosphorylation of amphiphysin I by minibrain kinase/dual-specificity tyrosine phosphorylation-regulated kinase, a kinase implicated in Down syndrome. J Biol Chem. 281(33):23712-24.
3. Sitz JH, 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.
4. Yamashita S, et al. (2009) Expression of dual-specificity tyrosine-(Y)-phosphorylation-regulated kinase 2 (DYRK2) can be a favorable prognostic marker in pulmonary adenocarcinoma. J Thorac Cardiovasc Surg. 138(6):1303-8.
5. Papadopoulos C, et al. (2011) Splice variants of the dual specificity tyrosine phosphorylation-regulated kinase 4 (DYRK4) differ in their subcellular localization and catalytic activity. J Biol Chem. 286(7):5494-505.