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Vol. 12, Issue 5, 1329-1340, May 2001
and
§
*Howard Hughes Medical Institute, Departments of
To investigate the targeting mechanism for proteins bound to the
mammalian Lin-7 (mLin-7) PDZ domain, we created receptor protein
chimeras composed of the carboxyl-terminal amino acids of LET-23 fused
to truncated nerve growth factor receptor/P75. mLin-7 bound to the
chimera with a wild-type LET-23 carboxyl-terminal tail (P75t-Let23WT),
but not a mutant tail (P75t-Let23MUT). In Madin-Darby canine kidney
(MDCK) cells, P75t-Let23WT localized to the basolateral plasma membrane
domain, whereas P75t-Let23MUT remained apical. Furthermore, mutant
mLin-7 constructs acted as dominant interfering proteins and inhibited
the basolateral localization of P75t-Let23WT. The mechanisms for this
differential localization were examined further, and, initially, we
found that P75t-Let23WT and P75t-Let23MUT were delivered equally to the
apical and basolateral plasma membrane domains. Although basolateral
retention of P75t-Let23WT, but not P75t-Let23MUT, was observed, the
greatest difference in receptor localization was seen in the rapid
trafficking of P75t-Let23WT to the basolateral plasma membrane domain
after endocytosis, whereas P75t-Let23MUT was degraded in lysosomes,
indicating that mLin-7 binding can alter the fate of endocytosed
proteins. Altogether, these data support a model for basolateral
protein targeting in mammalian epithelial cells dependent on
protein-protein interactions with mLin-7, and also suggest a dynamic
role for mLin-7 in endosomal sorting.
Internal Medicine and Biological
Chemistry, University of Michigan Medical School, Ann Arbor, Michigan
48109
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