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J Biol Chem, Vol. 274, Issue 35, 24579-24584, August 27, 1999
From the Renal Division, Department of Medicine, Brigham and
Women's Hospital and Harvard Medical School,
Boston, Massachusetts 02115
During development, tissue repair, and tumor
metastasis, both cell-cell dissociation and cell migration occur and
appear to be intimately linked, such as during epithelial
"scattering." Here we show that cell-cell dissociation during
scattering induced by hepatocyte growth factor (HGF) or activation of
the temperature-sensitive v-Src tyrosine kinase in MDCK cells can be
blocked by inhibiting the proteasome with lactacystin and MG132.
Although both proteins of the tight junction and the adherens junction
redistributed during cell scattering, proteasome inhibitors largely
prevented this process, resulting in the stabilization of Triton
X-100-insoluble tight junction proteins as well as adherens junction
proteins at sites of cell-cell contact. Proteasome inhibition also led to a decrease of E-cadherin turnover in 35S-labeled
cells. In addition, proteasome inhibition partly preserved cell
polarity, as determined by the subcellular distribution of Na+,K+-ATPase (basolateral marker) and gp135
(apical marker), and the structure of the subcortical actin ring, both
of which are normally disrupted during scattering. However, cells were
able to establish focal contacts, and single cell migration toward HGF
was unaffected by proteasome inhibition in quantitative assays,
indicating that cell-cell dissociation during scattering occurs
independently of anchorage-dependent cell migration. Thus,
a proteasome-dependent step during scattering induced by
HGF and pp60v-Src appears to be essential for cell-cell
dissociation, disassembly of junctional components, and (at least
indirectly) it also plays a role in the loss of protein polarity.
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