Recycling endosomes

Goldenring, James R.

doi:10.1016/j.ceb.2015.04.018

Cited by 132 publications

(129 citation statements)

References 52 publications

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“…This has been linked to signal amplification. Many internalized components are targeted to recycling endosomes and from there again to the cell surface or the tight junctions (40)(41)(42)(43)(44). The functions and the fate of internalized Nectin-1 remain to be identified.…”

Section: Discussionmentioning

confidence: 99%

Cbl E3 Ligase Mediates the Removal of Nectin-1 from the Surface of Herpes Simplex Virus 1-Infected Cells

Deschamps

Dogrammatzis

Mullick

et al. 2017

J Virol

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The Cbl E3 ligase has been linked to the down-modulation of surface signaling responses by inducing internalization of surface receptors. The adaptor protein CIN85 is a partner of Cbl that augments many of these interactions. Previously, an interaction was demonstrated between ICP0 and CIN85, which results in the removal of epidermal growth factor receptor (EGFR) from the surface of the infected cells with a concomitant attenuation of EGFR signaling. Here, we examined whether Cbl mediates the removal of the herpes simplex virus 1 (HSV-1) entry receptor Nectin-1 from the surface of infected cells. We found the following: (i) that Cbl, Nectin-1, and the viral glycoprotein D (gD) form a complex in infected cells; (ii) that during infection Nectin-1 is removed from the surface of the infected cells but is retained on the surface of cells that have been depleted of Cbl; and (iii) that in cells infected with a ΔICP0 mutant virus, Nectin-1 remained on the cell surface. Thus, Cbl is necessary but not sufficient for the removal of Nectin-1 from the cell surface. In addition, we observed that in Cbl-depleted cells there was enhanced entry after infection. These cells were susceptible to secondary infections by HSV-1. Viral entry in CIN85-depleted cells was only moderately enhanced compared to that in the Cbldepleted cells, suggesting that the Cbl-Nectin-1 interaction is likely the key to the downregulation of surface Nectin-1. The removal of the HSV-1 entry receptor Nectin-1 from the surface of the infected cells may be part of the strategy of the virus to efficiently spread to uninfected cells. IMPORTANCEThe Cbl E3 ligase suppresses surface signaling responses by inducing internalization of surface components. The targets of Cbl include such components as immune system receptors, growth factor receptors, adhesion, and cell-to-cell contact molecules. The immediate early protein ICP0 of herpes simplex virus 1 (HSV-1) interacts with CIN85, an adaptor protein that augments Cbl functions. The consequence of this interaction is the removal of the epidermal growth factor receptor (EGFR) from the surface of the infected cells with concomitant suppression of the EGF ligand signaling. The viral entry receptor Nectin-1 is also internalized during HSV-1 infection in a Cbl-dependent mechanism, and that increases the opportunity of the virus to spread to uninfected cells. The diversion of the Cbl/CIN85 endocytic machinery may be a strategy utilized by the virus to alter the cell surface pattern to prevent detrimental host responses.KEYWORDS Cbl E3 ligase, Nectin-1, endocytosis, ICP0, HSV-1, cell surface D uring herpes simplex virus 1 (HSV-1) infection, the immediate early protein ICP0 (infected cell protein 0) exerts two major sets of functions. First, ICP0 localizes in the nucleus immediately after its production and is involved in the blockage of the gene silencing machinery and provides an impediment to certain branches of innate immunity (1-4). After ICP0 accomplishes its major nuclear functions, it translocates to

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Section: Discussionmentioning

confidence: 99%

Cbl E3 Ligase Mediates the Removal of Nectin-1 from the Surface of Herpes Simplex Virus 1-Infected Cells

Deschamps

Dogrammatzis

Mullick

et al. 2017

J Virol

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“…Transported cargoes generally travel through a series of membrane-bound organelles, which include, in order: the ER-Golgi intermediate compartment (ERGIC), the Golgi, the trans-Golgi network (TGN) and, in some cases, the recycling endosomes (Palade, 1975, Goldenring, 2015, Guo et al, 2014, Brandizzi and Barlowe, 2013). This transport picture has emerged from the study of a small number of model cargoes, a typical example being the exogenous expression of the vesicular stomatitis virus glycoprotein (VSV-G).…”

Section: Introductionmentioning

confidence: 99%

Differential Regulation of Lipoprotein and Hepatitis C Virus Secretion by Rab1b

et al. 2017

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SUMMARY Secretory cells produce diverse cargoes, yet how they regulate concomitant secretory traffic remains insufficiently explored. Rab GTPases control intracellular vesicular transport. To map secretion pathways, we generated a library of lentivirus-expressed dominant-negative Rab mutants and used it in a large-scale screen to identify regulators of hepatic lipoprotein secretion. We identified several candidate pathways, including those mediated by Rab11 and Rab8. Surprisingly, inhibition of Rab1b, the major regulator of transport from the endoplasmic reticulum to the Golgi, differently affected the secretion of the very-low-density lipoprotein components ApoE and ApoB100, despite their final association on mature secreted lipoprotein particles. Since hepatitis C virus (HCV) incorporates ApoE and ApoB100 into its virus particle, we also investigated infectious HCV secretion, and show that its regulation by Rab1b mirrors that of ApoB100. These observations reveal differential regulation of hepatocyte secretion by Rab1b, and advance our understanding of lipoprotein assembly and lipoprotein and HCV secretion.

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“…Thus, sorting to the late endosome/lysosome originates primarily from the early sorting endosomes (Apodaca et al 1994). Established sorting destinations for membrane traffic out of the common/apical endosome of polarized cells include recycling back to the plasma membrane and by transcytosis to the contralateral membrane surface (Apodaca et al 1994; Tzaban et al 2009; Goldenring 2015). The mechanics for such selective and polarized sorting of cargo between recycling and transcytosis pathways likely overlaps with the machinery found in the trans- Golgi network (TGN) for the selective and polarized sorting of membrane proteins in the secretory pathway for membrane and secreted proteins of polarized cell types (Gan et al 2002; Gravotta et al 2007; Bay et al 2015).…”

Section: Specializations Of Endosomes Unique To Polarized Epithelialmentioning

confidence: 99%

Membrane Transport across Polarized Epithelia

García-Castillo

Chinnapen

Lencer

2017

Cold Spring Harb Perspect Biol

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Polarized epithelial cells line diverse surfaces throughout the body forming selective barriers between the external environment and the internal milieu. To cross these epithelial barriers, large solutes and other cargoes must undergo transcytosis, an endocytic pathway unique to polarized cell types, and significant for the development of cell polarity, uptake of viral and bacterial pathogens, transepithelial signaling, and immunoglobulin transport. Here, we review recent advances in our knowledge of the transcytotic pathway for proteins and lipids. We also discuss briefly the promise of harnessing the molecules that undergo transcytosis as vehicles for clinical applications in drug delivery.

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Recycling endosomes

Cited by 132 publications

References 52 publications

Cbl E3 Ligase Mediates the Removal of Nectin-1 from the Surface of Herpes Simplex Virus 1-Infected Cells

Cbl E3 Ligase Mediates the Removal of Nectin-1 from the Surface of Herpes Simplex Virus 1-Infected Cells

Differential Regulation of Lipoprotein and Hepatitis C Virus Secretion by Rab1b

Membrane Transport across Polarized Epithelia

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