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J. Biol. Chem., Vol. 269, Issue 28, 18267-18270, 07, 1994
L DaSilva, OM Howard, H Rui, RA Kirken and WL Farrar
Prolactin (PRL) has recently been demonstrated to induce tyrosine
phosphorylation and activation of the cytoplasmic tyrosine kinase JAK2 in
PRL-dependent Nb2 lymphoma cells. The present study represents an initial
effort to identify cytoplasmic regions of the PRL receptor (PRLR) that are
critical to growth signal generation and JAK2 activation. Variably
truncated rat PRLRs were stably expressed in the murine 32D cell line.
PRL-induced proliferation was mediated by the full-length receptor and the
mutant G328, which contains the membrane- proximal Homology Boxes 1 and 2
characteristic of hematopoietin receptors. In contrast, mutant receptors
lacking either Box 2 or both Boxes 1 and 2 were not capable of transmitting
a growth signal. The mitogenic capacity of the PRLR variants correlated
with JAK2 association and activation, as well as with induction of mRNA
levels for the growth-related gene ornithine decarboxylase. We conclude
that mitogenic competence of rat PRLRs resides within the first 94 amino
acids of the cytoplasmic domain. The data suggest that Homology Box 1/Box 2
region is critical to JAK2 phosphorylation and association with the PRLR.
These findings will serve as a basis for more detailed molecular
characterization of PRLR domains essential for JAK2 interaction and growth
signal generation.
Growth signaling and JAK2 association mediated by membrane-proximal cytoplasmic regions of prolactin receptors
Biological Carcinogenesis and Development Program, Program Resources Inc./DynCorp, Frederick, Maryland.
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