Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells

Farr, Glen A.; Hull, Michael; Mellman, Ira; Caplan, Michael J.

doi:10.1083/jcb.200901021

Cited by 87 publications

(86 citation statements)

References 58 publications

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“…Consistent with this possibility, we have demonstrated that ␣ 2B -AR and ␤ 2 -AR use different routes to move from the ER to the Golgi (25). Furthermore, a recent study has demonstrated that vesicular stomatitis virus glycoprotein and Na ϩ -K ϩ -ATPase follow different pathways to the basolateral cell surface in polarized cells (37). It is also possible that post-Golgi transport of ␣ 2B -AR and ␤ 2 -AR may be mediated through different transport vesicles that are differentially modulated by Rab8 GTPase.…”

Section: Discussionsupporting

confidence: 64%

Rab8 Interacts with Distinct Motifs in α2B- and β2-Adrenergic Receptors and Differentially Modulates Their Transport

Dong

Yang

Zhang

et al. 2010

Journal of Biological Chemistry

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The molecular mechanism underlying the post-Golgi transport of G protein-coupled receptors (GPCRs) remains poorly understood. Here we determine the role of Rab8 GTPase, which modulates vesicular protein transport between the trans-Golgi network (TGN) and the plasma membrane, in the cell surface targeting of ␣ 2B -and ␤ 2 -adrenergic receptors (AR). Transient expression of GDP-and GTP-bound Rab8 mutants and short hairpin RNA-mediated knockdown of Rab8 more potently inhibited the cell surface expression of ␣ 2B -AR than ␤ 2 -AR. The GDP-bound Rab8(T22N) mutant attenuated ERK1/2 activation by ␣ 2B -AR, but not ␤ 2 -AR, and arrested ␣ 2B -AR in the TGN compartment. Co-immunoprecipitation revealed that both ␣ 2B -AR and ␤ 2 -AR physically interacted with Rab8 and glutathione S-transferase fusion protein pulldown assays demonstrated that Rab8 interacted with the C termini of both receptors. Interestingly, mutation of the highly conserved membrane-proximal C terminus dileucine motif selectively blocked ␤ 2 -AR interaction with Rab8, whereas mutation of residues (T22N) of a chimeric ␤ 2 -AR carrying the ␣ 2B -AR C terminus was similar to ␣ 2B -AR. These data provide strong evidence indicating that Rab8 GTPase interacts with distinct motifs in the C termini of ␣ 2B -AR and ␤ 2 -AR and differentially modulates their traffic from the TGN to the cell surface.

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Section: Discussionsupporting

confidence: 64%

Rab8 Interacts with Distinct Motifs in α2B- and β2-Adrenergic Receptors and Differentially Modulates Their Transport

Dong

Yang

Zhang

et al. 2010

Journal of Biological Chemistry

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“…The tag binds covalently to O 6 -benzylguanine (BG), resulting in the irreversible transfer of the substituted benzyl group to the reactive thiol within the SNAP tag. BG derivatives bearing fluorophores, biotin, or other groups can be used to label a SNAP-tagged protein (Farr et al, 2009;Maurel et al, 2010;Sun et al, 2011;Lukinavičius et al, 2013).…”

Section: Resultsmentioning

confidence: 99%

The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135

Stoops¹,

Hull²,

Olesen³

et al. 2015

J Gen Physiol

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“…On endocytosis from the oligodendroglial plasma membrane, PLP strictly enters the LE/Lys compartment and is never observed in RE (Winterstein et al, 2008). In epithelial cells, it has been demonstrated that a subset of cargos transit through RE intermediates on their biosynthetic route from the Golgi to the cell surface (Ang et al, 2004;Cresawn et al, 2007;Desclozeaux et al, 2008;Farr et al, 2009). Interestingly, the basolateral transport of those cargos traversing RE depends on VAMP3 (Fields et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

“…Taking into account our in vitro data, we, however, assume that redundant transport pathways compensate lack of VAMP3 and VAMP7 function to achieve delivery of PLP. The establishment of multiple surface trafficking pathways involving endosomal compartments and redundancy among SNAREs is common to cells with sophisticated membrane compartment organization such as epithelial cells, adipocytes, and neurons (Borisovska et al, 2005;Farr et al, 2009;Zhao et al, 2009), allowing the cells to maintain their major functions within the organ despite the loss of individual components.…”

Section: Role Of Vamp3 and Vamp7 In Myelinationmentioning

confidence: 99%

Transport of the Major Myelin Proteolipid Protein Is Directed by VAMP3 and VAMP7

Feldmann¹,

Amphornrat²,

Schönherr³

et al. 2011

J. Neurosci.

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CNS myelination by oligodendrocytes requires directed transport of myelin membrane components and a timely and spatially controlled membrane expansion. In this study, we show the functional involvement of the R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (R-SNARE) proteins VAMP3/cellubrevin and VAMP7/TI-VAMP in myelin membrane trafficking. VAMP3 and VAMP7 colocalize with the major myelin proteolipid protein (PLP) in recycling endosomes and late endosomes/lysosomes, respectively. Interference with VAMP3 or VAMP7 function using small interfering RNA-mediated silencing and exogenous expression of dominantnegative proteins diminished transport of PLP to the oligodendroglial cell surface. In addition, the association of PLP with myelin-like membranes produced by oligodendrocytes cocultured with cortical neurons was reduced. We furthermore identified Syntaxin-4 and Syntaxin-3 as prime acceptor Q-SNAREs of VAMP3 and VAMP7, respectively. Analysis of VAMP3-deficient mice revealed no myelination defects. Interestingly, AP-3␦-deficient mocha mice, which suffer from impaired secretion of lysosome-related organelles and missorting of VAMP7, exhibit a mild dysmyelination characterized by reduced levels of select myelin proteins, including PLP. We conclude that PLP reaches the cell surface via at least two trafficking pathways with distinct regulations: (1) VAMP3 mediates fusion of recycling endosomederived vesicles with the oligodendroglial plasma membrane in the course of the secretory pathway; (2) VAMP7 controls exocytosis of PLP from late endosomal/lysosomal organelles as part of a transcytosis pathway. Our in vivo data suggest that exocytosis of lysosomerelated organelles controlled by VAMP7 contributes to myelin biogenesis by delivering cargo to the myelin membrane.

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Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells

Cited by 87 publications

References 58 publications

Rab8 Interacts with Distinct Motifs in α2B- and β2-Adrenergic Receptors and Differentially Modulates Their Transport

Rab8 Interacts with Distinct Motifs in α2B- and β2-Adrenergic Receptors and Differentially Modulates Their Transport

The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135

Transport of the Major Myelin Proteolipid Protein Is Directed by VAMP3 and VAMP7

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