Cargo Sorting in the Endocytic Pathway: A Key Regulator of Cell Polarity and Tissue Dynamics

Eaton, Suzanne; Martı́n-Belmonte, Fernando

doi:10.1101/cshperspect.a016899

Cited by 66 publications

(67 citation statements)

References 111 publications

(126 reference statements)

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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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“…120 The identities of the apical and basolateral membrane further critically rely on a polarized trafficking machinery that drives the targeted transport of vesicles carrying distinct lipids and proteins. 122 The delivery of these lipids and proteins to the correct plasma membrane is ensured by diverse apical and basolateral sorting signals and mechanisms. 122 Tight junctions that prevent diffusion of proteins and lipids from one membrane domain to the other are required to maintain membrane identity.…”

Section: Generation and Maintenance Of Epithelial Polaritymentioning

confidence: 99%

“…122 The delivery of these lipids and proteins to the correct plasma membrane is ensured by diverse apical and basolateral sorting signals and mechanisms. 122 Tight junctions that prevent diffusion of proteins and lipids from one membrane domain to the other are required to maintain membrane identity. 120 Finally, the polarization of individual cells is translated into the arrangement of higher-order cell structures to build the proper epithelial tissue architecture.…”

Section: Generation and Maintenance Of Epithelial Polaritymentioning

confidence: 99%

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Apicobasal polarity of brain endothelial cells

Worzfeld

Schwaninger

2015

J Cereb Blood Flow Metab

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Normal brain homeostasis depends on the integrity of the blood-brain barrier that controls the access of nutrients, humoral factors, and immune cells to the CNS. The blood-brain barrier is composed mainly of brain endothelial cells. Forming the interface between two compartments, they are highly polarized. Apical/luminal and basolateral/abluminal membranes differ in their lipid and (glyco-)protein composition, allowing brain endothelial cells to secrete or transport soluble factors in a polarized manner and to maintain blood flow. Here, we summarize the basic concepts of apicobasal cell polarity in brain endothelial cells. To address potential molecular mechanisms underlying apicobasal polarity in brain endothelial cells, we draw on investigations in epithelial cells and discuss how polarity may go awry in neurological diseases.

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“…In many cases, internalized cell surface materials are recycled back to the cell surface. The balance between endocytosis and recycling is an important mechanism that regulates diverse cellular processes such as cytokinesis (Albertson et al, 2005), cell junction formation (Chalmers and Whitley, 2012), polarity establishment (Eaton and Martin-Belmonte, 2014), and integrin signaling (Wickström and Fassler, 2011). While endocytosis and recycling networks have been extensively characterized in mammalian cells, endocytosis and recycling were largely overlooked in plants for some time because of the false notion that endocytosis is suppressed under the high turgor pressure that pushes the plasma membrane (PM) tightly against the cell walls of plant cells.…”

Section: Introductionmentioning

confidence: 99%

CELLULOSE SYNTHASE INTERACTIVE1 Is Required for Fast Recycling of Cellulose Synthase Complexes to the Plasma Membrane in Arabidopsis

et al. 2015

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Cargo Sorting in the Endocytic Pathway: A Key Regulator of Cell Polarity and Tissue Dynamics

Cited by 66 publications

References 111 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

Apicobasal polarity of brain endothelial cells

CELLULOSE SYNTHASE INTERACTIVE1 Is Required for Fast Recycling of Cellulose Synthase Complexes to the Plasma Membrane in Arabidopsis

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