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2014 ; 127
(Pt 20
): 4457-69
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Galectin-4-mediated transcytosis of transferrin receptor
#MMPMID25179596
Perez Bay AE
; Schreiner R
; Benedicto I
; Rodriguez-Boulan EJ
J Cell Sci
2014[Oct]; 127
(Pt 20
): 4457-69
PMID25179596
show ga
Some native epithelia, for example, retinal pigment epithelium (RPE) and kidney
proximal tubule (KPT), constitutively lack the basolateral sorting adaptor AP-1B;
this results in many basolateral plasma membrane proteins being repositioned to
the apical domain, where they perform essential functions for their host organs.
We recently reported the underlying apical polarity reversal mechanism: in the
absence of AP-1B-mediated basolateral sorting, basolateral proteins are shuttled
to the apical plasma membrane through a transcytotic pathway mediated by the
plus-end kinesin KIF16B. Here, we demonstrate that this apical transcytotic
pathway requires apical sorting of basolateral proteins, which is mediated by
apical signals and galectin-4. Using RPE and KPT cell lines, and AP-1B-knockdown
MDCK cells, we show that mutation of the N-glycan linked to N727 in the
basolateral marker transferrin receptor (TfR) or knockdown of galectin-4 inhibits
TfR transcytosis to apical recycling endosomes and the apical plasma membrane,
and promotes TfR lysosomal targeting and subsequent degradation. Our results
report a new role of galectins in basolateral to apical epithelial transcytosis.
|Adaptor Protein Complex 1/genetics/*metabolism
[MESH]
|Adaptor Protein Complex beta Subunits/genetics/*metabolism
[MESH]