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(Received for publication, July 16, 1996, and in revised form, September 3, 1996)
From the The mitogen-activated protein (MAP)
kinase family includes extracellular signal-regulated kinase (ERK),
c-Jun NH2-terminal kinase/stress-activated protein
kinase (JNK/SAPK) and p38/RK/CSBP (p38) as structurally and
functionally distinct enzyme classes. 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. Although
stress-induced activation of p54 SAPK
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27205-27208
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
and
Geneva Biomedical Research Institute, Glaxo
Wellcome Research and Development S. A., CH-1228 Plan-les-Ouates,
Geneva, Switzerland, the § Genetics Laboratory, Biochemistry
Department, South Parks Road, Oxford, OX1 3QU, United Kingdom, and the
Cancer Research Campaign Centre For Cell and Molecular Biology,
Chester Beatty Laboratories, The Institute of Cancer Research, Fulham
Road, London, SW3 6JB, United Kingdom
, p46 SAPK
(JNK1) or p38 MAP
kinases is abolished upon co-transfection with increasing amounts of
M3/6 plasmid, epidermal growth factor-stimulated ERK1 is remarkably
insensitive even to the highest levels of M3/6 expression obtained. In
contrast to M3/6, the dual specificity phosphatase MKP-3 is selective
for inactivation of ERK family MAP kinases. Low level expression of
MKP-3 blocks totally epidermal growth factor-stimulated ERK1, whereas
stress-induced activation of p54 SAPK and p38 MAP kinases is
inhibited only partially under identical conditions. Selective
regulation by M3/6 and MKP-3 was also observed upon chronic MAP kinase
activation by constitutive p21ras GTPases. Hence, although M3/6
expression effectively blocked p54 SAPK activation by p21rac
(G12V), ERK1 activated by p21ras (G12V) was insensitive to this
phosphatase. ERK1 activation by oncogenic p21ras was, however,
blocked totally by co-expression of MKP-3. This is the first report
demonstrating reciprocally selective inhibition of different MAP
kinases by two distinct dual specificity phosphatases.
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