scholarly journals Phosphorylation-Dependent Activation of the ESCRT Function of ALIX in Cytokinetic Abscission and Retroviral Budding

2016 ◽  
Vol 36 (3) ◽  
pp. 331-343 ◽  
Author(s):  
Sheng Sun ◽  
Le Sun ◽  
Xi Zhou ◽  
Chuanfen Wu ◽  
Ruoning Wang ◽  
...  
Keyword(s):  
Retroviral Budding

scholarly journals Parallels Between Cytokinesis and Retroviral Budding: A Role for the ESCRT Machinery

Science ◽  
2007 ◽  
Vol 316 (5833) ◽  
pp. 1908-1912 ◽  
Author(s):  
J. G. Carlton ◽  
J. Martin-Serrano
Keyword(s):  
Escrt Machinery ◽  
Retroviral Budding

scholarly journals TANK-Binding Kinase 1 Attenuates PTAP-Dependent Retroviral Budding through Targeting Endosomal Sorting Complex Required for Transport-I

2011 ◽  
Vol 186 (5) ◽  
pp. 3023-3030 ◽  
Author(s):  
Qi Da ◽  
Xuanming Yang ◽  
Youli Xu ◽  
Guangxia Gao ◽  
Genhong Cheng ◽  
...  
Keyword(s):  
Endosomal Sorting ◽  
Retroviral Budding

ESCRTs and human disease

2009 ◽  
Vol 37 (1) ◽  
pp. 167-172 ◽  
Author(s):  
Suraj Saksena ◽  
Scott D. Emr
Keyword(s):  
Human Disease ◽  
Protein Sorting ◽  
Critical Role ◽  
Multivesicular Body ◽  
Human Diseases ◽  
Down Regulation ◽  
Endosomal Sorting ◽  
Retroviral Budding

The ESCRT (endosomal sorting complex required for transport) machinery plays a critical role in receptor down-regulation, retroviral budding, and other normal and pathological processes. The ESCRT components are conserved in all five major subgroups of eukaryotes. This review summarizes the growing number of links identified between ESCRT-mediated protein sorting in the MVB (multivesicular body) pathway and various human diseases.

Host factors involved in retroviral budding and release

2011 ◽  
Vol 9 (7) ◽  
pp. 519-531 ◽  
Author(s):  
Juan Martin-Serrano ◽  
Stuart J. D. Neil
Keyword(s):  
Host Factors ◽  
Retroviral Budding

scholarly journals Phosphorylation-Dependent Activation of the ESCRT Function of ALIX in Cytokinetic Abscission and Retroviral Budding

2016 ◽  
Vol 37 (6) ◽  
pp. 581 ◽  
Author(s):  
Sheng Sun ◽  
Le Sun ◽  
Xi Zhou ◽  
Chuanfen Wu ◽  
Ruoning Wang ◽  
...  
Keyword(s):  
Retroviral Budding

scholarly journals Insertion of Capsid Proteins from Nonenveloped Viruses into the Retroviral Budding Pathway

2001 ◽  
Vol 75 (14) ◽  
pp. 6527-6536
Author(s):  
Neel K. Krishna ◽  
John W. Wills
Keyword(s):  
Simian Virus 40 ◽  
Simian Virus ◽  
Capsid Proteins ◽  
Normal Density ◽  
Uniform Size ◽  
Gag Proteins ◽  
Rous Sarcoma ◽  
Satellite Tobacco Mosaic Virus ◽  
Sarcoma Virus ◽  
Retroviral Budding

ABSTRACT Retroviral Gag proteins direct the assembly and release of virus particles from the plasma membrane. The budding machinery consists of three small domains, the M (membrane-binding), I (interaction), and L (late or “pinching-off”) domains. In addition, Gag proteins contain sequences that control particle size. For Rous sarcoma virus (RSV), the size determinant maps to the capsid (CA)-spacer peptide (SP) sequence, but it functions only when I domains are present to enable particles of normal density to be produced. Small deletions throughout the CA-SP sequence result in the release of particles that are very large and heterogeneous, even when I domains are present. In this report, we show that particles of relatively uniform size and normal density are released by budding when the size determinant and I domains in RSV Gag are replaced with capsid proteins from two unrelated, nonenveloped viruses: simian virus 40 and satellite tobacco mosaic virus. These results indicate that capsid proteins of nonenveloped viruses can interact among themselves within the context of Gag and be inserted into the retroviral budding pathway merely by attaching the M and L domains to their amino termini. Thus, the differences in the assembly pathways of enveloped and nonenveloped viruses may be far simpler than previously thought.

scholarly journals Assembly of the AAA ATPase Vps4 on ESCRT-III

2010 ◽  
Vol 21 (6) ◽  
pp. 1059-1071 ◽  
Author(s):  
Anna Shestakova ◽  
Abraham Hanono ◽  
Stacey Drosner ◽  
Matt Curtiss ◽  
Brian A. Davies ◽  
...  
Keyword(s):  
Complex Network ◽  
Protein Trafficking ◽  
Interaction Network ◽  
Aaa Atpase ◽  
Key Enzyme ◽  
In Vivo Analysis ◽  
Retroviral Budding ◽  
High Degree

Vps4 is a key enzyme that functions in endosomal protein trafficking, cytokinesis, and retroviral budding. Vps4 activity is regulated by its recruitment from the cytoplasm to ESCRT-III, where the protein oligomerizes into an active ATPase. The recruitment and oligomerization steps are mediated by a complex network of at least 12 distinct interactions between Vps4, ESCRT-III, Ist1, Vta1, and Did2. The order of events leading to active, ESCRT-III–associated Vps4 is poorly understood. In this study we present a systematic in vivo analysis of the Vps4 interaction network. The data demonstrated a high degree of redundancy in the network. Although no single interaction was found to be essential for the localization or activity of Vps4, certain interactions proved more important than others. The most significant among these were the binding of Vps4 to Vta1 and to the ESCRT-III subunits Vps2 and Snf7. In our model we propose the formation of a recruitment complex in the cytoplasm that is composed of Did2-Ist1-Vps4, which upon binding to ESCRT-III recruits Vta1. Vta1 in turn is predicted to cause a rearrangement of the Vps4 interactions that initiates the assembly of the active Vps4 oligomer.

scholarly journals When in Need of an ESCRT: The Nature of Virus Assembly Sites Suggests Mechanistic Parallels between Nuclear Virus Egress and Retroviral Budding

Viruses ◽  
2021 ◽  
Vol 13 (6) ◽  
pp. 1138
Author(s):  
Kevin M. Rose
Keyword(s):  
Virus Assembly ◽  
Cellular Membrane ◽  
Particle Assembly ◽  
Endosomal Sorting ◽  
Nuclear Egress ◽  
Viral Particles ◽  
Nuclear Particle ◽  
Retroviral Budding ◽  
Cellular Compartments ◽  
Hsv 1

The proper assembly and dissemination of progeny virions is a fundamental step in virus replication. As a whole, viruses have evolved a myriad of strategies to exploit cellular compartments and mechanisms to ensure a successful round of infection. For enveloped viruses such as retroviruses and herpesviruses, acquisition and incorporation of cellular membrane is an essential process during the formation of infectious viral particles. To do this, these viruses have evolved to hijack the host Endosomal Sorting Complexes Required for Transport (ESCRT-I, -II, and -III) to coordinate the sculpting of cellular membrane at virus assembly and dissemination sites, in seemingly different, yet fundamentally similar ways. For instance, at the plasma membrane, ESCRT-I recruitment is essential for HIV-1 assembly and budding, while it is dispensable for the release of HSV-1. Further, HSV-1 was shown to recruit ESCRT-III for nuclear particle assembly and egress, a process not used by retroviruses during replication. Although the cooption of ESCRTs occurs in two separate subcellular compartments and at two distinct steps for these viral lifecycles, the role fulfilled by ESCRTs at these sites appears to be conserved. This review discusses recent findings that shed some light on the potential parallels between retroviral budding and nuclear egress and proposes a model where HSV-1 nuclear egress may occur through an ESCRT-dependent mechanism.

scholarly journals The VPS-20 subunit of the endosomal sorting complex ESCRT-III exhibits an open conformation in the absence of upstream activation

2015 ◽  
Vol 466 (3) ◽  
pp. 625-637 ◽  
Author(s):  
Amber L. Schuh ◽  
Michael Hanna ◽  
Kyle Quinney ◽  
Lei Wang ◽  
Ali Sarkeshik ◽  
...  
Keyword(s):  
Membrane Repair ◽  
Endosomal Sorting ◽  
Escrt Machinery ◽  
Cell Extracts ◽  
Open Conformation ◽  
Membrane Reorganization ◽  
Plasma Membrane Repair ◽  
Retroviral Budding ◽  
Vacuolar Protein

Members of the endosomal sorting complex required for transport (ESCRT) machinery function in membrane remodelling processes during multivesicular endosome (MVE) biogenesis, cytokinesis, retroviral budding and plasma membrane repair. During luminal vesicle formation at endosomes, the ESCRT-II complex and the ESCRT-III subunit vacuolar protein sorting (VPS)-20 play a specific role in regulating assembly of ESCRT-III filaments, which promote vesicle scission. Previous work suggests that Vps20 isoforms, like other ESCRT-III subunits, exhibits an auto-inhibited closed conformation in solution and its activation depends on an association with ESCRT-II specifically at membranes [1]. However, we show in the present study that Caenorhabditis elegans ESCRT-II and VPS-20 interact directly in solution, both in cytosolic cell extracts and in using recombinant proteins in vitro. Moreover, we demonstrate that purified VPS-20 exhibits an open extended conformation, irrespective of ESCRT-II binding, in contrast with the closed auto-inhibited architecture of another ESCRT-III subunit, VPS-24. Our data argue that individual ESCRT-III subunits adopt distinct conformations, which are tailored for their specific functions during ESCRT-mediated membrane reorganization events.

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