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J. Biol. Chem., Vol. 278, Issue 20, 18617-18627, May 16, 2003
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From the Tumor necrosis factor-
Characterization of Growth Factor-induced Serine
Phosphorylation of Tumor Necrosis Factor-
Converting Enzyme and of
an Alternatively Translated Polypeptide*
§¶,
, and
Departments of Growth and Development, and
Anatomy, Programs in Cell Biology and Developmental Biology, University
of California, San Francisco, California 94143, the
§ Department of Physiology and Biophysics, University of
Medicine and Dentistry of New Jersey Robert Wood Johnson Medical
School, and Cancer Institute of New Jersey,
Piscataway, New Jersey 08854, and Howard Hughes Medical
Institute and Department of Medicine, University of California,
San Francisco, California 94143
converting enzyme
(TACE) is a prototype member of the adamalysin family of transmembrane
metalloproteases that effects ectodomain cleavage and release of many
transmembrane proteins, including transforming growth factor-.
Growth factors that act through tyrosine kinase receptors, as well as
other stimuli, induce shedding through activation of the Erk
mitogen-activated protein (MAP) kinase pathway without the need of new
protein synthesis. How MAP kinase regulates shedding by TACE is not
known. We now report that the cytoplasmic domain of TACE is
phosphorylated in response to growth factor stimulation. We also
identified a naturally expressed smaller polypeptide corresponding to
most of the cytoplasmic domain of TACE. This protein, which we named
SPRACT, is derived through alternative translation of the TACE-coding
sequence and is, similarly to TACE, phosphorylated in response to
growth factor and phorbol 12-myristate 13-acetate stimulation.
Phosphoamino acid analysis revealed that growth factor-induced
phosphorylation of TACE occurs only on serine and not on threonine or
tyrosine. Tryptic mapping experiments coupled with site-directed
mutagenesis identified Ser819 as the major target of
growth factor-induced phosphorylation, whereas Ser791
undergoes dephosphorylation in response to growth factor stimulation. The phosphorylation of Ser819, but not the
dephosphorylation of Ser791, depends on activation of the
Erk MAP kinase pathway. Increased SPRACT expression or mutation of the
TACE cytoplasmic domain to inactivate growth factor-induced
phosphorylation did not detectably affect growth factor-induced
shedding of transmembrane transforming growth factor- by TACE. The
roles of SPRACT and the cytoplasmic phosphorylation of TACE remain to
be defined.
*
This work was supported by National Institutes of Health
Grants CA54826 and DE13904 (Project 1) (to R. D.), a University of Medicine and Dentistry of New Jersey Robert Wood Johnson Medical School
start-up grant, and a University of Medicine and Dentistry of New
Jersey Foundation Seed Grant (to H. F.).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.
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