Role of the epithelial cell-specific clathrin adaptor complex AP-1B in cell polarity

Fölsch, Heike

doi:10.1080/21592799.2015.1074331

Cited by 34 publications

(21 citation statements)

References 94 publications

(143 reference statements)

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“…Indeed, membrane recruitment of AP-2 is strictly dependent on PI(4,5)P2 and thus AP-2 should be absent from areas that are enriched in PI(3,4,5)P3 (Collins et al, 2002). In contrast, AP-1B is recruited by PI(3,4,5)P3 (Fields et al, 2010), most likely in addition to Arf6 (Fölsch, 2015b;Shteyn et al, 2011) thus explaining why AP-2 and AP-1B localize to different areas in cell protrusions. In contrast, AP-1A is recruited onto PI(4)P-positive membranes and therefore absent from focal adhesions and the plasma membrane (Wang et al, 2003).…”

Section: Putative Regulation Of Ap-1b's Endocytic Activitymentioning

confidence: 99%

“…Major sorting stations for the polarized delivery of cargos to the plasma membrane are the trans-Golgi network (TGN) during biosynthesis and recycling endosomes (REs) for sorting of endocytic cargos and biosynthetic cargos that reach REs from the TGN (Ang et al, 2004;Ang and Fölsch, 2012;Fölsch et al, 2009). Basolateral sorting in REs depends on AP-1B (Fölsch, 2015b). AP-1B is a heterotetrameric clathrin adaptor that shares its two large g and b1 and its small s1 subunit with AP-1A .…”

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%

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AP-1B facilitates endocytosis during cell migration

Kell¹,

Ang²,

Pigati³

et al. 2019

Preprint

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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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Section: Putative Regulation Of Ap-1b's Endocytic Activitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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AP-1B facilitates endocytosis during cell migration

Kell¹,

Ang²,

Pigati³

et al. 2019

Preprint

Self Cite

View full text Add to dashboard Cite

show abstract

“…Although µ1A and µ1B are about 80% identical on the amino acid level, they nevertheless lead to the localization of AP-1A and AP-1B to different compartments, with AP-1A at the trans-Golgi network, and AP-1B in REs. In addition, they don’t form mixed clathrin-coated vesicles and fulfill largely non-overlapping functions [reviewed in (6)]. Furthermore, I found that AP-1B triggers the recruitment of exocyst complex components onto the REs for incorporation into AP-1B vesicles (2).…”

mentioning

confidence: 99%

“…Presently, we don’t know much about how PI(3,4,5)P 3 is generated and what role AP-1B plays in its accumulation. Moreover, Rab8, and Rab10 may negatively regulate Arf6 and thus AP-1B function [reviewed in (6)]. We are interested in finding out more about possible cross-talk among the small GTPases that localize in REs.…”

mentioning

confidence: 99%