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Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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.

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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.

ATP Driven Pumps III: V-type Pumps

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...

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Updated: Jun 17, 2026

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

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

Published on: August 9, 2024

Vpr and its interactions with cellular proteins.

Vicente Planelles¹, Serge Benichou

¹Division of Cell Biology and Immunology, Department of Pathology, University of Utah School of Medicine, 15 North Medical Drive East #2100-Room 2520, Salt Lake City, Utah 84112, USA. vicente.planelles@path.utah.edu

Current Topics in Microbiology and Immunology

|December 17, 2009

Summary

This summary is machine-generated.

The HIV-1 Vpr protein interacts with numerous cellular proteins, influencing viral replication and host cell functions like cell cycle arrest and viral DNA nuclear import. Understanding these interactions is key to comprehending HIV-1 pathogenesis.

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Published on: September 2, 2019

Area of Science:

Virology
Molecular Biology
Cell Biology

Background:

Human Immunodeficiency Virus type 1 (HIV-1) viral regulatory protein, Vpr, is small and multifunctional.
Vpr plays a role in various cellular processes, including G2 cell cycle arrest, apoptosis, and viral DNA nuclear import.
Understanding Vpr's interactions with host cell proteins is crucial for elucidating its impact on viral replication and pathogenesis.

Purpose of the Study:

To review and summarize the cellular proteins that interact with HIV-1 Vpr.
To discuss the significance of these Vpr-cellular protein interactions in relation to Vpr's known functions.
To explore the implications of these interactions for HIV-1 replication and cellular effects.

Main Methods:

Literature review of studies reporting interactions between HIV-1 Vpr and cellular proteins.
Analysis of the functional consequences of identified Vpr-host protein interactions.
Synthesis of information regarding Vpr's role in cell cycle regulation, apoptosis, and viral DNA trafficking.

Main Results:

Numerous cellular proteins have been identified to interact with HIV-1 Vpr.
These interactions are linked to Vpr's diverse functions, including modulation of the cell cycle (G2 arrest), apoptosis induction, and enhancement of viral DNA nuclear import in non-dividing cells.
Vpr's interaction with cellular factors contributes to viral replication fidelity and efficiency.

Conclusions:

The multifunctional nature of HIV-1 Vpr is mediated through interactions with a wide array of cellular proteins.
These interactions are critical for key steps in the HIV-1 life cycle, such as reverse transcription and nuclear import.
Further investigation into Vpr-host protein complexes may reveal novel therapeutic targets for HIV-1 infection.