Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

2.0K
2.0K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

8.6K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.6K
Cell-surface Signaling01:21

Cell-surface Signaling

53.7K
Hormones—or any molecule that binds to a receptor, known as a ligand—that are lipid-insoluble (water-soluble) are not able to diffuse across the cell membrane. In order to be able to affect a cell without entering it, these hormones bind to receptors on the cell membrane. When a first messenger, a hormone, binds to a receptor, a signal cascade is set off, causing second messengers, proteins inside the cell, to become activated, resulting in downstream effects.
53.7K
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

2.7K
Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
2.7K
Intracellular Hormone Receptors01:08

Intracellular Hormone Receptors

58.3K
Lipid-soluble hormones diffuse across the plasma and nuclear membrane of target cells to bind to their specific intracellular receptors. These receptors act as transcription factors that regulate gene expression and protein synthesis in the target cell
58.3K
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

7.1K
Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
7.1K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Rad18 suppresses the late step of human immunodeficiency virus type 1 replication.

bioRxiv : the preprint server for biology·2025
Same author

ASCT2 inhibits HIV-1 infectivity by promoting the incorporation of a gp160/ASCT2 complex into virions.

mBio·2025
Same author

Transcriptional regulation of the HIV-1 inhibitory factor human mannose receptor 1 by the myeloid-specific transcription factor PU.1.

Journal of virology·2023
Same author

Macrophage-Derived Factors with the Potential to Contribute to Pathogenicity of HIV-1 and HIV-2: Role of CCL-2/MCP-1.

Viruses·2023
Same author

Human Mannose Receptor 1 Attenuates HIV-1 Infectivity in a Virus Isolate-Specific Manner.

Viruses·2023
Same author

HIV-1 Vpr Induces Degradation of Gelsolin, a Myeloid Cell-Specific Host Factor That Reduces Viral Infectivity by Inhibiting the Expression and Packaging of the HIV-1 Env Glycoprotein.

mBio·2023

Related Experiment Video

Updated: Jan 5, 2026

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

794

Vpr and Its Cellular Interaction Partners: R We There Yet?

Helena Fabryova1, Klaus Strebel2

  • 1Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bldg. 4, Room 312, 4 Center Drive, MSC 0460, Bethesda, MD 20892, USA. helena.fabryova@nih.gov.

Cells
|October 27, 2019
PubMed
Summary

The viral protein R (Vpr) acts as a molecular adapter, crucial for lentivirus replication in macrophages and pathogenesis. This review summarizes cellular proteins targeted by Vpr.

Keywords:
HIV-1Vpraccessory geneshost restriction factors

More Related Videos

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
16:36

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

Published on: May 18, 2009

15.1K
Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes
07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

4.3K

Related Experiment Videos

Last Updated: Jan 5, 2026

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
08:54

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

Published on: August 9, 2024

794
Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
16:36

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

Published on: May 18, 2009

15.1K
Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes
07:22

Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

Published on: January 12, 2024

4.3K

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Vpr is a lentiviral accessory protein packaged into virus particles.
  • Its role in viral fitness is context-dependent, being critical in macrophages and in vivo.
  • Vpr functions as a molecular adapter, not an enzyme, modulating viral and cellular processes.

Purpose of the Study:

  • To review and summarize the cellular proteins targeted by the Vpr protein.
  • To consolidate current knowledge on Vpr-interacting factors.

Main Methods:

  • Literature review of studies investigating Vpr interactions.
  • Analysis of Vpr's role in viral replication and pathogenesis.

Main Results:

  • Vpr interacts with numerous cellular proteins.
  • These interactions are key to Vpr's function in specific cellular environments and pathogenesis.

Conclusions:

  • Vpr's function is mediated through its interactions with cellular proteins.
  • Understanding these interactions is vital for comprehending lentiviral pathogenesis and Vpr's role.