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J. Biol. Chem., Vol. 276, Issue 7, 4531-4534, February 16, 2001
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From the University Research Centre for Neuroendocrinology and MRC
Centre for Synaptic Plasticity, University of Bristol, Marlborough
Street, Bristol, BS2 8HW, the § Department of Biochemistry,
University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, and the
¶ Department of Medicine, Adrian Building. University of
Leicester. Leicester LE1 7RH, United Kingdom
Studies in non-neuronal cells show that c-Jun
N-terminal kinases (JNK) play a key role in apoptotic cell death. In
some neurons JNK is also thought to initiate cell death by the
activation of c-Jun. JNK inhibition has been achieved pharmacologically
by inhibiting upstream kinases, but there has been no direct
demonstration that inhibition of JNK can prevent neuronal death. We
have therefore examined whether the JNK binding domain (JBD) of
JNK-interacting protein-1 (JIP-1, a scaffold protein and specific
inhibitor of JNK) can inhibit c-Jun phosphorylation and support the
survival of sympathetic neurons deprived of NGF. We show that
expression of the JBD in >80% of neurons was sufficient to prevent
the phosphorylation of c-Jun and its nuclear accumulation as well as
abrogate neuronal cell death induced by NGF deprivation. JBD expression
also preserved the capacity of mitochondria to reduce MTT.
Interestingly, although the PTB domain of JIP was reported to
interact with rhoGEF, expression of the JBD domain was sufficient to
localize the protein to the membrane cortex and growth cones.
Hence, JNK activation is a key event in apoptotic death induced
by NGF withdrawal, where its point of action lies upstream of
mitochondrial dysfunction.
ACCELERATED PUBLICATION
Inhibition of JNK by Overexpression of the JNK Binding
Domain of JIP-1 Prevents Apoptosis in Sympathetic Neurons*
,§,
, and
*
This work was supported in part by grants from the BBSRC,
the Wellcome Trust (to A. M. T. and L. X.), and the South and West Research Directorate.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The first two authors contributed equally to this work.
To whom correspondence may be addressed. Tel.:
44-117-928-3452; Fax: 44-117-928-3315; E-mail:
james.uney@bristol.ac.uk (to J. B. U.) or Tel.: 44-1223-339319; Fax:
44-1223-333345; E-mail: amt@mole.bio.cam.ac.uk (to
A. M. T.).
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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