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Vol. 14, Issue 4, 1346-1354, April 2003
and§
Proteasomal activity is required for Met receptor degradation after
acute stimulation with hepatocyte growth factor (HGF). Inhibition of
proteasomal activity with lactacystin leads to a block in the endocytic
trafficking of Met such that the receptor fails to reach late
endosomes/lysosomes, where degradation by acid-dependent proteases
takes place (Hammond et al., 2001). In this article, we
have biochemically determined Met internalization rates from the cell
surface and shown that lactacystin does not inhibit the initial
HGF-dependent internalization step of Met. Instead, it promotes the
recycling pathway from early endosomes at the expense of sorting to
late endosomes, thereby ensuring rapid return of internalized Met to
the cell surface. We have used this perturbation of Met endosomal
sorting by lactacystin to examine the consequences for HGF-dependent
signaling outputs. In control cells HGF-dependent receptor
autophosphorylation reaches a maximal level over 5-10 min but then
attenuates over the ensuing 50 min. Furthermore, Met dephosphorylation
can be kinetically dissociated from Met degradation. In
lactacystin-treated cells, we observe a failure of Met
dephosphorylation as well as Met degradation. Elements of the
mitogen-activated protein kinase cascade, downstream of receptor
activation, show a normal kinetic profile of phosphorylation, indicating that the mitogen-activated protein kinase pathway can attenuate in the face of sustained receptor activation. The
HGF-dependent phosphorylation of a receptor substrate that is localized
to clathrin-coated regions of sorting endosomes, Hrs, is dramatically
reduced by lactacystin treatment. Reduction of cellular Hrs levels by
short interfering RNA modestly retards Met degradation and markedly prevents the attenuation of Met phosphorylation. HGF-dependent Hrs
phosphorylation and Met dephosphorylation may provide signatures for
retention of the receptor in coated regions of the endosome implicated
in sorting to lysosomes.
Physiological Laboratory, University of
Liverpool, Liverpool, L69 3BX, United Kingdom; and
Van Andel Institute, Grand Rapids, Michigan
49503
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