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-Secretase Cleavage and Nuclear Localization of ErbB-4 Receptor Tyrosine Kinase
Chang-Yuan Ni,1M. Paul Murphy,3Todd E. Golde,3Graham Carpenter12*
ErbB-4 is a transmembrane receptor tyrosine kinase that regulates
cell proliferation and differentiation. After binding ofits ligand
heregulin (HRG) or activation of protein kinase C (PKC)by
12-O-tetradecanoylphorbol-13-acetate (TPA), the
ErbB-4 ectodomainis cleaved by a metalloprotease. We now report a
subsequent cleavageby -secretase that releases the ErbB-4
intracellular domain fromthe membrane and facilitates its
translocation to the nucleus.-Secretase cleavage was prevented by
chemical inhibitors or adominant negative presenilin. Inhibition of
-secretase also preventedgrowth inhibition by HRG. -Secretase
cleavage of ErbB-4 may representanother mechanism for receptor
tyrosine kinase-mediated signaling.
1 Department of Biochemistry,
2 Department of Medicine, Vanderbilt University
School of Medicine, Nashville, TN 37232, USA.
3 Department of Neuroscience and Pharmacology, Mayo
Clinic Jacksonville, Jacksonville, FL 32224, USA.
*
To whom correspondence should be addressed. E-mail:
graham.carpenter{at}mcmail.vanderbilt.edu
The editors suggest the following Related Resources on Science sites:
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PERSPECTIVES
Carl-Henrik Heldin and Johan Ericsson (7 December 2001) Science294 (5549), 2111.
[DOI: 10.1126/science.1067628] |Summary »|Full Text »|PDF »
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-Secretase Cleavage and Nuclear Localization of ErbB-4 Receptor Tyrosine Kinase
-secretase that releases the ErbB-4
intracellular domain from the membrane and facilitates its
translocation to the nucleus.