Scientific background: |
DUSP3(Dual-specificity phosphatase 3), also called VHR, is a member of the dual specificity protein
phosphatase subfamily. DUSPs constitute a large heterogeneous subgroup of the type I cysteine-based
protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate
both tyrosine and serine/threonine residues. DUSP3 contains the consensus DUSP C-terminal catalytic
domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase
phosphatase) class of DUSPs. The DUSP3 gene is mapped on 17q21.31. Confocal microscopy
demonstrated that phosphorylated VHR accumulated at the immune synapse between the T cell and
the antigen-presenting cell in the presence of antigen. Tyrosine phosphorylation of VHR affects
protein-protein interaction, subcellular location, or substrate targeting, given that tyr138 is located on
the opposite side of the VHR catalytic center. |
References: |
Alonso, A., Rahmouni, S., Williams, S., van Stipdonk, M., Jaroszewski, L., Godzik, A., Abraham, R.
T., Schoenberger, S. P., Mustelin, T. Tyrosine phosphorylation of VHR phosphatase by
ZAP-70. Nature Immun. 4: 44-48, 2003.
2. Ishibashi, T., Bottaro, D. P., Chan, A., Miki, T., Aaronson, S. A. Expression cloning of a human
dual-specificity phosphatase. Proc. Nat. Acad. Sci. 89: 12170-12174, 1992.
3. Patterson, K. I., Brummer, T., O'Brien, P. M., Daly, R. J. Dual-specificity phosphatases: critical
regulators with diverse cellular targets.Biochem. J. 418: 475-489, 2009. |