DUSP2
DUSP2 (dual specificity phosphatase 2, also known as PAC-1) is a nuclear dual specificity phosphatase that removes phosphate groups from threonine and tyrosine residues on MAP kinases. It acts as a negative regulator of MAPK signalling, inactivating ERK1 and ERK2. Browse Assay Genie's current range of DUSP2 research reagents below, or read on for the biology behind the target.
DUSP2 inactivates its target kinases by dephosphorylating both phosphoserine/threonine and phosphotyrosine residues. In the case of MAPK1 (ERK2), the enzyme dephosphorylates both the phosphorylated threonine and tyrosine residues, with removal of phosphotyrosine proceeding slightly faster than removal of phosphothreonine. Through this activity, the DUSP2 protein negatively regulates members of the mitogen-activated protein kinase superfamily (MAPK/ERK, SAPK/JNK and p38), which are associated with cellular proliferation and differentiation. Its characterised role is the inactivation of ERK1 and ERK2.
DUSP2 belongs to the protein-tyrosine phosphatase family, in the non-receptor class dual specificity subfamily, and is classed by HGNC among the MAP kinase phosphatases. Different dual specificity phosphatases show distinct substrate specificities for individual MAP kinases, different tissue distribution and subcellular localisation, and different modes of inducible expression in response to extracellular stimuli. DUSP2 is predominantly expressed in haematopoietic tissues and is localised in the nucleus. The DUSP2 gene has a mouse ortholog, Dusp2.
The enzyme carries two EC classifications, reflecting its activity towards both phosphoserine/threonine and phosphotyrosine substrates. The alias PAC-1 is commonly used in the literature. Comparing DUSP2 with other MAP kinase phosphatases is a useful way to explore how cells tune the strength and duration of MAPK signalling.
DUSP2 inactivates ERK1 and ERK2 by dephosphorylating threonine and tyrosine residues, making it a relevant node for studying negative feedback in MAP kinase pathways.
DUSP2 is predominantly expressed in haematopoietic tissues, so it is of interest when examining kinase regulation in blood and immune cell lineages.
By restraining MAPK/ERK, SAPK/JNK and p38 pathways linked to proliferation and differentiation, DUSP2 informs studies of how cell fate decisions are controlled.
Dual specificity phosphatases differ in MAP kinase substrate preference, localisation and inducibility, and DUSP2 provides a nuclear example for comparative work.
DUSP2 is a nuclear dual specificity phosphatase that dephosphorylates both threonine and tyrosine residues in MAPK1, with phosphotyrosine removed slightly faster than phosphothreonine. It inactivates ERK1 and ERK2 and so negatively regulates MAP kinase signalling linked to proliferation and differentiation.
The HGNC full name is dual specificity phosphatase 2, and UniProt lists it as dual specificity protein phosphatase 2. The alias PAC-1 is also used. DUSP2 belongs to the HGNC group of MAP kinase phosphatases, and it carries EC numbers 3.1.3.16 and 3.1.3.48.
A mouse ortholog, Dusp2, is recorded for the human gene. Human DUSP2 is one of several dual specificity phosphatases that differ in MAP kinase specificity, tissue distribution and localisation. Check the datasheet of any product for its validated reactivity.
Other dual specificity phosphatases and MAP kinase phosphatases involved in regulating MAPK signalling.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q05923; product specifications from Assay Genie datasheets.