Rotavirus receptor proteins Hsc70 and integrin αvβ3 are located in the lipid microdomains of animal intestinal cells

Ca, Guerrero; Lp, Moreno

doi:10.4149/av_2012_01_63

Cited by 21 publications

(18 citation statements)

References 11 publications

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“…In the present study we did not look for NCL phosphorylation; however, we showed that ␤ 3 Tyr 773 phosphorylation is required for NCL cell surface localization. ␣ v ␤ 3 integrin is found to form a complex with hsc70 in lipid raft microdomains of the cytoplasmatic membrane of susceptible intestinal epithelial cells, and both act as receptors for rotavirus entry (62). Therefore, it is tempting to speculate that ␣ v ␤ 3 and hsc70 may cooperate for cell surface NCL localization and in that case direct or indirect NCL phosphorylation by protein kinase C-and casein kinase 2 may have a role.…”

Section: Discussionmentioning

confidence: 99%

Interplay between αvβ3 Integrin and Nucleolin Regulates Human Endothelial and Glioma Cell Migration

Κουτσιούμπα

Polytarchou

Courty

et al. 2013

Journal of Biological Chemistry

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Background: Cell surface nucleolin (NCL) is a promising target for development of anticancer agents. Results: A novel pathway that includes ␣ ␤ 3 integrin and leads to cell surface NCL localization and cell migration has been identified. Conclusion: ␣ ␤ 3 can be used as a biomarker for the use of NCL antagonists. Significance: This pathway is active in endothelial and glioma cells, as well as in human glioblastomas.

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Section: Discussionmentioning

confidence: 99%

Interplay between αvβ3 Integrin and Nucleolin Regulates Human Endothelial and Glioma Cell Migration

Κουτσιούμπα

Polytarchou

Courty

et al. 2013

Journal of Biological Chemistry

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“…HSP gp96 (HSP90b1), an HSP90 paralogue present in the endoplasmic reticulum of lymphocytes, binds to the aL integrin subunit and maintains cell-surface expression of aL integrins but not a4 integrins [17]. Hsc70 (HSP73) and the integrin avb3 associate together as a complex in lipid raft microdomains of the cytoplasmic membranes of epithelial cells [18]. Extracellular HSP60 specifically binds to the integrin a3b1 expressed by breast carcinoma cells and activates its adhesive function [19].…”

Section: Introductionmentioning

confidence: 99%

Leukocyte integrin α4β7 associates with heat shock protein 70

et al. 2015

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The leukocyte integrin cell adhesion molecules α4β7 and αEβ7 mediate the homing and retention of lymphocytes to the gut, and sites of inflammation. Here we have identified heat shock protein 70 (HSP70) as a major protein that associates with the cytoplasmic domain of the integrin β7 subunit. HSPs are molecular chaperones that protect cells from stress but more recently have been reported to also regulate cell adhesion and invasion via modulation of β1, β2, and β3 integrins and integrin-associated signalling molecules. Several HSP70 isoforms including HSP70-3, HSP70-1L, HSP70-8, and HSP70-9 were specifically precipitated from T cells by a bead-conjugated β7 subunit cytoplasmic domain peptide and subsequently identified by high-resolution liquid chromatography-tandem mass spectrometry. In confirmation, the β7 subunit was co-immunoprecipitated from a T cell lysate by an anti-HSP70 antibody. Further, recombinant human HSP70-1a was precipitated by β7 cytoplasmic domain-coupled beads. The HSP70 inhibitor KNK437 decreased the expression of HSP70 without affecting the expression of the β7 integrin. It significantly inhibited α4β7-mediated adhesion of T cells to mucosal addressin cell adhesion molecule 1 (MAdCAM-1), suggesting HSP70 is critical for maintaining β7 integrin signalling function. The functional implications of the association of β7 integrins with the different isoforms of HSP70 warrants further investigation.

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“…In a study conducted with Co-IP followed by protein identification with MS, Hsc70 was found to exist on the plasma membranes of C6/36 and Vero cells (Ren et al, 2007), implying that Hsc70 may be important in receptor-dependent endocytosis. It is further presumed that Hsc70 might be one component of the receptor for rotaviruses infecting animal intestinal cells because Hsc70 levels increase after infection and form a complex with integrin avb3 in the lipid raft microdomains of the cytoplasmic membrane (Guerrero & Moreno, 2012). Since JEV and Hsc70 proteins co-localize and attach to the surface of C6/36 cells, this molecule has been proposed to serve as the receptor for JEV entry into host cells (Ren et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Heat shock cognate protein 70 isoform D is required for clathrin-dependent endocytosis of Japanese encephalitis virus in C6/36 cells

Chuang

Yang

Chen

et al. 2015

Journal of General Virology

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Japanese encephalitis virus (JEV), one of encephalitic flaviviruses, is naturally transmitted by mosquitoes. During infection, JEV generally enters host cells via receptor-mediated clathrindependent endocytosis that requires the 70 kDa heat-shock protein (Hsp70). Heat-shock cognate protein 70 (Hsc70) is one member of the Hsp70 family and is constitutively expressed; thus, it may be expressed under physiological conditions. In C6/36 cells, Hsc70 is upregulated in response to JEV infection. Since Hsc70 shows no relationship with viruses attaching to the cell surface, it probably does not serve as the receptor according to our results in the present study. In contrast, Hsc70 is evidently associated with virus penetration into the cell and resultant acidification of intracellular vesicles. It suggests that Hsc70 is highly involved in clathrin-mediated endocytosis, particularly at the late stage of viral entry into host cells. Furthermore, we found that Hsc70 is composed of at least three isoforms, including B, C and D; of these, isoform D helps JEV to penetrate C6/36 cells via clathrin-mediated endocytosis. This study provides relevant evidence that sheds light on the regulatory mechanisms of JEV infection in host cells, especially on the process of clathrin-mediated endocytosis.

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Rotavirus receptor proteins Hsc70 and integrin αvβ3 are located in the lipid microdomains of animal intestinal cells

Cited by 21 publications

References 11 publications

Interplay between αvβ3 Integrin and Nucleolin Regulates Human Endothelial and Glioma Cell Migration

Interplay between αvβ3 Integrin and Nucleolin Regulates Human Endothelial and Glioma Cell Migration

Leukocyte integrin α4β7 associates with heat shock protein 70

Heat shock cognate protein 70 isoform D is required for clathrin-dependent endocytosis of Japanese encephalitis virus in C6/36 cells

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