DUSP3 / VHR Protein

Dual Specificity Phosphatase 3 / Vaccinia H1-related phosphatase

DUSP3 / VHR Products

DUSP3 / VHR Protein, Recombinant

Molecule	Species	Description	Cat. No
DUSP3/VHR	Human	DUSP3/VHR Protein, Recombinant, with GST Tag	10114-H20B

DUSP3 / VHR cDNA Clone

Molecule	Species	Description	Cat. No
DUSP3/VHR	Human	Human DUSP3/VHR cDNA Clone / ORF Clone	HG10114-M

DUSP3 / VHR Related Areas

Enzyme>>Phosphatase & Regulator>>DUSP3/VHR

Signal Transduction>>Phosphatase & Regulator>>DUSP3/VHR

DUSP3 / VHR Alternative Names

DUSP3, VHR [Homo sapiens]

Dusp3, VHR, RP23-398F7.3, 2210015O03Rik, 5031436O03Rik, T-DSP11 [Mus musculus]

DUSP3 / VHR Background

Vaccinia H1-related phosphatase (VHR) is classified as a dual-specificity phosphatase (DUSP), and the other name is dual-specificity phosphatase 3 (DUSP3). DUSPs are a heterogeneous group of protein phosphatases that can dephosphorylate both phosphotyrosine and phosphoserine/phosphothreonine residues within the one substrate. Unlike typical DUSPs, VHR lacks mitogen-activated protein kinase (MAPK)-binding domain, and shows poor activity against MAPKs. VHR often act on bisphosphorylated protein substrates, it displays a strong preference for dephosphorylating phosphotyrosine residues over phosphothreonine residues. VHR has been identified as a novel regulator of extracellular regulated kinases (ERKs). VHR is responsible for the rapid inactivation of ERK following stimulation and for its repression in quiescent cells. VHR is a negative regulator of the Erk and Jnk pathways in T cells and, therefore, may play a role in aspects of T lymphocyte physiology that depend on these kinases.

DUSP3 / VHR Related Studies

1. Todd J.L, et al. (1999) Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway. J. Biol. Chem. 274: 13271-80.
2. Alonso A, et al. (2001) Inhibitory role for dual specificity phosphatase VHR in T cell antigen receptor and CD28-induced Erk and Jnk activation. J Biol Chem. 276(7): 4766-71.
3. Schumacher MA, et al. (2002) Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase. Biochemistry. 41(9): 3009-17.
4. Patterson KI, et al. (2009) Dual-specificity phosphatases: critical regulators with diverse cellular targets. Biochem J. 2009 Mar 15;418(3): 475-89.