DUSP26 Human

Dual Specificity Phosphatase 26 (DUSP26) is a member of the tyrosine phosphatase family of proteins. It exhibits dual specificity by dephosphorylating tyrosine as well as serine and threonine residues . This enzyme plays a crucial role in the regulation of intracellular signaling pathways, which in turn influence a broad range of physiological processes .

DUSP26 is an atypical dual specificity phosphatase with a range of physiological substrates, including the Mitogen-Activated Protein Kinases (MAPKs) . The protein is known to inactivate MAPK1 and MAPK3, leading to the dephosphorylation of heat shock factor protein 4 and a reduction in its DNA-binding activity . Additionally, DUSP26 inhibits MAP kinase p38 by dephosphorylating it and inhibits p38-mediated apoptosis in anaplastic thyroid cancer cells .

The expression of DUSP26 varies depending on the cellular context. It has been described as both a tumor suppressor and an oncogene . This dual role is context-dependent and highlights the complexity of its function in different tissues and conditions.

DUSP26 is heavily implicated in cancer, where it displays both tumor-suppressive and tumor-promoting properties . The residues that govern DUSP26 substrate specificity are yet to be determined; however, recent evidence suggests that interactions with a binding partner may be required for DUSP26 catalytic activity .

The regulation of DUSP26 involves its interaction with various binding partners and its ability to dephosphorylate key signaling molecules. This regulation is crucial for maintaining cellular homeostasis and responding to internal or external stimuli .

Recombinant Human DUSP26 is a denatured protein with a N-Terminal His-tag and corresponds to the amino acids 1-211 of Human DUSP26 . It is produced in E. coli and is used in various research applications to study its function and regulation .