HIV-1 Vpu inhibits accumulation of the envelope glycoprotein within clathrin-coated, Gag-containing endosomes

Damme, Nanette Van

doi:10.1111/j.1462-5822.2007.01101.x

Cited by 41 publications

(52 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this case, partitioning of HM1.24 into lipid raft domains on the cell surface seems to help promote encounters with assembling HIV-1 particles (11), because removal of the GPI anchor completely abolished the ability of tetherin to inhibit Vpu-deleted HIV-1 virion release. Notably, the expression of Eps15-DIII did not block the endosomal accumulation of either Gag or HIV envelope glycoprotein in HeLa cells expressing vpu-negative virus (61). These results, coupled with the data presented in this study, may further strengthen our hypothesis that HM1.24 is internalized by a novel endocytic mechanism, which is independent of the typical AP-2 adaptor complex.…”

Section: Discussionsupporting

confidence: 78%

HM1.24 Is Internalized from Lipid Rafts by Clathrin-mediated Endocytosis through Interaction with α-Adaptin

Masuyama

Kuronita

Tanaka

et al. 2009

Journal of Biological Chemistry

130

178

View full text Add to dashboard Cite

HM1.24/Bst2/CD317 is a protein highly expressed in multiple myeloma cells and has unique topology with two membrane anchor domains, an NH 2 -terminal transmembrane domain and a glycosylphosphatidylinositol attached to the COOH terminus. We show here that human HM1.24 is localized not only on the cell surface but also in the trans-Golgi network and/or recycling endosomes, where it resides in detergent-resistant microdomains, lipid rafts. In contrast to other glycosylphosphatidylinositol-anchored proteins, HM1.24 was internalized from lipid rafts on the cell surface by clathrin-mediated endocytosis. Interestingly, a non-canonical tyrosine-based motif, which contains two tyrosine residues, Tyr-6 and Tyr-8, present in the NH 2 -terminal cytoplasmic tail, was essential for endocytosis through interaction with an ␣-adaptin, but not 2-subunit, of the AP-2 complex. Indeed, an appendage domain of ␣-adaptin was identified as a protein interacting with the cytoplasmic tail of HM1.24. Furthermore, overexpression of the appendage domain of ␣-adaptin in cells depleted of ␣-adaptin could rescue the clathrin-mediated endocytosis of HM1.24 but not of the transferrin receptor. Taken together, our findings suggest that clathrin-dependent endocytosis of human HM1.24 from the cell surface lipid rafts is mediated by direct interaction with ␣-adaptin.

show abstract

Section: Discussionsupporting

confidence: 78%

HM1.24 Is Internalized from Lipid Rafts by Clathrin-mediated Endocytosis through Interaction with α-Adaptin

Masuyama

Kuronita

Tanaka

et al. 2009

Journal of Biological Chemistry

130

178

View full text Add to dashboard Cite

show abstract

“…CD317 ͉ host restriction ͉ tetherin ͉ virus assembly V pu is an 81-aa type 1 integral membrane protein (1, 2) that has been shown to cause proteasomal degradation of CD4 (3,4), enhance the release of virions from infected cells (5), and prevent endocytosis of nascent viral particles (6)(7)(8)(9)(10)(11). These latter biological activities of Vpu are mechanistically distinct from CD4 degradation and involve different structural domains in Vpu.…”

Section: Hiv-1 Vpu Enhances the Release Of Virions From Infected Cellsmentioning

confidence: 99%

Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface down-modulation and intracellular depletion

Miyagi

Andrew

Kao

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

205

281

View full text Add to dashboard Cite

HIV-1 Vpu enhances the release of virions from infected cells. Recent work identified Bst-2/CD317/tetherin as a host factor whose inhibitory activity on viral release is counteracted by Vpu. A current working model proposes that Bst-2 inhibits virus release by tethering viral particles to the cell surface. Here, we analyzed endogenous Bst-2 with respect to its effect on virus release from HeLa cells, T cells, and macrophages. We noted significant cell type-dependent variation in Bst-2 expression. Vpu caused a reduction in Bst-2 expression in transfected HeLa cells and long-term infected macrophages. However, Vpu expression did not result in cell surface down-modulation of Bst-2 or a reduction in intracellular Bst-2 expression in CEMx174 or H9 cells, yet virus replication in these cells was Vpu-responsive. Surprisingly, Bst-2 was undetectable in cell-free virions that were recovered from the surface of HeLa cells by physical shearing, suggesting that a tethering model may not explain all of the functional properties of Bst-2. Taken together we conclude that enhancement of virus release by Vpu does not, at least in CEMx174 and H9 cells, require cell surface down-modulation or intracellular depletion of Bst-2, nor does it entail exclusion of Bst-2 from viral particles.

show abstract

“…It is also known that interaction of AP1 with the matrix domain of human immunodeficiency virus type 1 Gag protein promotes viral release (5). In addition, Vpu inhibits the endosomal accumulation of the human immunodeficiency virus type 1 structural proteins Env and Gag, which is known to enhance viral assembly and release at the plasma membrane (39). Furthermore, large hepatitis delta antigen (HDAg-L) encoded by the hepatitis delta virus (HDV) has recently been identified as a novel clathrin adaptor-like protein (18).…”

mentioning

confidence: 99%

Clathrin-Mediated Post-Golgi Membrane Trafficking in the Morphogenesis of Hepatitis Delta Virus

Huang

Chang²,

Yang

et al. 2009

J Virol

View full text Add to dashboard Cite

Clathrin is involved in the endocytosis and exocytosis of cellular proteins and the process of virus infection.We have previously demonstrated that large hepatitis delta antigen (HDAg-L) functions as a clathrin adaptor, but the detailed mechanisms of clathrin involvement in the morphogenesis of hepatitis delta virus (HDV) are not clear. In this study, we found that clathrin heavy chain (CHC) is a key determinant in the morphogenesis of HDV. HDAg-L with a single amino acid substitution at the clathrin box retained nuclear export activity but failed to interact with CHC and to assemble into virus-like particles. Downregulation of CHC function by a dominant-negative mutant or by short hairpin RNA reduced the efficiency of HDV assembly, but not the secretion of hepatitis B virus subviral particles. In addition, the coexistence of a cell-permeable peptide derived from the C terminus of HDAg-L significantly interfered with the intracellular transport of HDAg-L. HDAg-L, small HBsAg, and CHC were found to colocalize with the trans-Golgi network and were highly enriched on clathrin-coated vesicles. Furthermore, genotype II HDV, which assembles less efficiently than genotype I HDV does, has a putative clathrin box in its HDAg-L but interacted only weakly with CHC. The assembly efficiency of the various HDV genotypes correlates well with the CHC-binding activity of their HDAg-Ls and coincides with the severity of disease outcome. Thus, the clathrin box and the nuclear export signal at the C terminus of HDAg-L are potential new molecular targets for HDV therapy.

show abstract

HIV-1 Vpu inhibits accumulation of the envelope glycoprotein within clathrin-coated, Gag-containing endosomes

Cited by 41 publications

References 48 publications

HM1.24 Is Internalized from Lipid Rafts by Clathrin-mediated Endocytosis through Interaction with α-Adaptin

HM1.24 Is Internalized from Lipid Rafts by Clathrin-mediated Endocytosis through Interaction with α-Adaptin

Vpu enhances HIV-1 virus release in the absence of Bst-2 cell surface down-modulation and intracellular depletion

Clathrin-Mediated Post-Golgi Membrane Trafficking in the Morphogenesis of Hepatitis Delta Virus

Contact Info

Product

Resources

About