Molecular Mechanisms of Apical and Basolateral Sorting in Polarized Epithelial Cells

Weisz, Ora A.; Fölsch, Heike

doi:10.1007/978-1-4939-3366-2_7

Cited by 4 publications

(3 citation statements)

References 139 publications

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“…In polarized cells, such as those that make up epithelia, integral membrane proteins are differentially targeted to apical or basolateral plasma membrane domains ( Weisz and Fölsch, 2020 ). In these cells, several signals have been identified that confer sorting.…”

Section: Introductionmentioning

confidence: 99%

GOPC facilitates the sorting of syndecan-1 in polarized epithelial cells

Ford

Burd

2022

MBoC

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Section: Introductionmentioning

confidence: 99%

GOPC facilitates the sorting of syndecan-1 in polarized epithelial cells

Ford

Burd

2022

MBoC

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“…This monolayer architecture has to be maintained throughout life to avoid diseases such as metastatic cancer and polycystic kidney disease (Mellman and Nelson, 2008). To ensure this, epithelial cells continuously sort membrane receptors and adhesion molecules to either surface domain (Weisz and Fölsch, 2016;Weisz and Rodriguez-Boulan, 2009). However, little is known about the involvement or behavior of the polarized sorting machinery during epithelial wound-healing.…”

Section: Introductionmentioning

confidence: 99%

“…Since its discovery, LLC-PK1 cell lines with or without exogenous expression of µ1B to restore AP-1B function have been widely used to analyze polarized protein sorting (Fölsch, 2015a). Like other members of the family of heterotetrameric adaptor complexes such as AP-1A, AP-2, AP-3 and AP-4, AP-1B directly recognizes cargos with YxxØ motifs via µ1B and [D/E]xxxL[L/I] motifs, LL-motifs for short, through a shared surface between s1 and g adaptin (Fölsch, 2015b;Ohno et al, 1999;Weisz and Fölsch, 2016).…”

Section: Introductionmentioning

confidence: 99%

AP-1B facilitates endocytosis during cell migration

Kell¹,

Ang²,

Pigati³

et al. 2019

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The epithelial cell-specific clathrin adaptor AP-1B has a well-established role in polarized sorting of cargos to the basolateral membrane. Here we demonstrate a novel function for AP-1B during collective cell migration of epithelial sheets. We show that AP-1B colocalized with b1 integrin in focal adhesions during cell migration using confocal microscopy and total internal reflection fluorescence (TIRF) microscopy on fixed specimens. Further, AP-1B labeling in cell protrusion was distinct from labeling for the canonical endocytic adaptor complex AP-2. Using stochastic optical reconstruction microscopy (STORM) and live TIRF imaging we identified numerous AP-1B-coated structures at or close to the plasma membrane in cell protrusions.Importantly, immuno-electron microscopy (EM) showed AP-1B in clathrin-coated pits and budding vesicles at the plasma membrane during cell migration. Our data therefore established a novel function for AP-1B in endocytosis. We further show that b1 integrin was dependent on AP-1B and its co-adaptor, autosomal recessive hypercholesterolemia protein (ARH), for sorting to the basolateral membrane. Notably, we found that expression of AP-1B (and ARH) slowed epithelial-cell migration, and qRT-PCR analysis of human epithelial-derived cell lines revealed a loss of AP-1B expression in highly metastatic cancer cells indicating that AP-1B-facilitated endocytosis during cell migration might be an anti-cancer mechanism.

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