Question: Is protein M3/6 a dual specificity phosphatase?

Context:
Involvement of the dual-specificity phosphatase M3/6 in c-Jun N-terminal kinase inactivation following cerebral ischemia in the rat hippocampus.
The results revealed upregulation of dual-specificity phosphatase M3/6 (DUSP8) activity at 4 h of reperfusion in rat hippocampi. 
This study examines the molecular mechanism underlying JNK dephosphorylation and inactivation evoked by dual-specificity phosphates following cerebral ischemia.
Phosphatases play a particularly important role in this respect, by tightly controlling MAPK phosphorylation and activation. M3/6 (DUSP8) is a dual-specificity phosphatase implicated in the dephosphorylation and inactivation of JNK and, to a lesser extent, p38 MAPKs and is found in a complex with these kinases, along with other pathway components, held together by scaffold proteins. 
Dual-specificity phosphatases (DUSPs) play a very important role in these events by modulating the extent of JNK phosphorylation and activation and thus regulating cellular responses to stress. M3/6 (DUSP8) is one of the dual-specificity protein phosphatases with distinct specificity towards JNK.
M3/6 is a dual-specificity phosphatase selective for JNK [7, 8]. 
Here we describe two new dual specificity phosphatases of the CL100/MKP-1 family that are selective for inactivating ERK or JNK/SAPK and p38 MAP kinases when expressed in COS-7 cells. M3/6 is the first phosphatase of this family to display highly specific inactivation of JNK/SAPK and p38 MAP kinases. 
We previously demonstrated that the dual specificity phosphatases (DSPs) MKP7 and M3/6 bind the scaffold JNK-interacting protein-1 (JIP-1) and inactivate the bound subset of JNK (1).
the dual-specificity phosphatase M3/6
 dual-specificity phosphatase M3/6 (DUSP8)
M3/6 (DUSP8) is a dual-specificity phosphatase implicated in the dephosphorylation and inactivation of JNK 
the M3/6 dual-specificity phosphatase
M3/6 (DUSP8) is one of the dual-specificity protein phosphatases with distinct specificity towards JNK
M3/6 is a dual-specificity phosphatase selective for JNK
The dual specificity phosphatases M3/6 and MKP-3 are highly selective for inactivation of distinct mitogen-activated protein kinases.
Phosphorylation of the M3/6 dual-specificity phosphatase enhances the activation of JNK by arsenite.
Indeed, expanded polyglutamine impaired the solubility of the dual-specificity JNK phosphatase M3/6.
Regulation of dual-specificity phosphatases M3/6 and hVH5 by phorbol esters.
M3/6 (DUSP8) is one of the dual-specificity protein phosphatases with distinct specificity towards JNK.
M3/6 is a dual-specificity phosphatase selective for JNK [7, 8]
M3/6 (DUSP8) is one of the dual-specificity protein phosphatases with distinct specificity towards JNK
Here we describe how diverse cellular stresses affect differently the stability and activity of a JNK-inactivating dual-specificity threonine-tyrosine phosphatase M3/6
M3/6 is a dual-specificity phosphatase selective for JNK [7, 8]
Regulation of dual-specificity phosphatases M3/6 and hVH5 by phorbol esters. Analysis of a delta-like domain.
The results revealed upregulation of dual-specificity phosphatase M3/6 (DUSP8) activity at 4 h of reperfusion in rat hippocampi
Indeed, expanded polyglutamine impaired the solubility of the dual-specificity JNK phosphatase M3/6
Here we report that JIP-1 also binds the dual-specificity phosphatases MKP7 and M3/6 via a region independent of its JNK binding domain.
Differential regulation of M3/6 (DUSP8) signaling

Answer: M3/6 (DUSP8) is a dual-specificity phosphatase implicated in the dephosphorylation and inactivation of JNK and, to a lesser extent, p38 MAPKs.
Yes. Phosphatases play a particularly important role in this respect, by tightly controlling MAPK phosphorylation and activation. M3/6 (DUSP8) is a dual-specificity phosphatase implicated in the dephosphorylation and inactivation of JNK and, to a lesser extent, p38 MAPKs and is found in a complex with these kinases, along with other pathway components, held together by scaffold proteins.
The protein M3/6 (DUSP8) is a dual-specificity phosphatase implicated in the dephosphorylation and inactivation of JNK
Exact answer: yes