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- W2891176887 abstract "SUMMARY Apical polarity of cystic fibrosis transmembrane conductance regulator (CFTR) is essential for solute and water transport in secretory epithelia and can be impaired in human diseases. Maintenance of apical polarity in the face of CFTR non-polarized delivery and compromised apical retention of mutant CFTRs lacking PDZ-domain protein (NHERF1) interaction, remains enigmatic. Here we show that basolateral CFTR delivery originates from biosynthetic (~35%) and endocytic (~65%) recycling missorting. Basolateral channels are retrieved via basolateral-to-apical transcytosis, enhancing CFTR apical expression by two-fold and suppressing its degradation. CFTR transcytosis is microtubule-dependent but independent of Myo5B-, Rab11- and NHERF1 binding to its C-terminal DTRL motif in airway epithelia. Increased basolateral delivery due to compromised apical recycling and accelerated internalization upon impaired NHERF1-CFTR association is largely counterbalanced by CFTR efficient basolateral internalization and apical transcytosis. Thus, transcytosis represents a previously unrecognized but indispensable mechanism for maintaining CFTR apical polarity by attenuating its constitutive and mutation-induced basolateral missorting." @default.
- W2891176887 created "2018-09-27" @default.
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- W2891176887 date "2018-09-07" @default.
- W2891176887 modified "2023-09-25" @default.
- W2891176887 title "Transcytosis maintains CFTR apical polarity in the face of constitutive and mutation-induced basolateral missorting" @default.
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- W2891176887 doi "https://doi.org/10.1101/411322" @default.
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