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J Biol Chem, Vol. 273, Issue 45, 29381-29388, November 6, 1998
1 Integrin Mediate
Polarization in Madin-Darby Canine Kidney Cells by Selective
Basolateral Stabilization
From the Department of Cell Biology, University of Geneva, 1211 Geneva, Switzerland
In Madin-Darby canine kidney cells, newly
synthesized apical and basolateral membrane proteins are generally
transported directly to their respective cell surface domain due to
targeting determinants that mediate sorting in the Golgi complex. In
several basolateral membrane proteins, these targeting determinants
reside in the cytoplasmic domains. We show here that basolateral
expression of the human 
5
1 integrin
in stably transfected Madin-Darby canine kidney cells is also mediated
by the cytoplasmic domains. Distinct regions in both cytoplasmic
domains were found to be sufficient to mediate basolateral expression
independently from one another. Unexpectedly, newly synthesized
wild-type 51 and basolaterally expressed
chimeras containing the cytoplasmic domain of either 5
or 1 were integrated into both cell surface domains,
preferentially apically, during biosynthesis. The apical pools of
wild-type integrin and chimeric subunits were found to become quickly
degraded, whereas the basolateral pools were stabilized. Thus, the
cytoplasmic domains of the 51 integrin
are independently sufficient to mediate sorting by selective
basolateral stabilization.
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