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

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.2K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
7.2K
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

5.9K
GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
5.9K
Lipids as Anchors01:32

Lipids as Anchors

8.0K
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
8.0K
Rab Proteins01:14

Rab Proteins

5.4K
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...
5.4K
Protein-protein Interfaces02:04

Protein-protein Interfaces

15.0K
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...
15.0K
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

3.8K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
3.8K

You might also read

Related Articles

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

Sort by
Same author

The LEDGIN GS-9822 inhibits HIV-2 infection and enhances HIV-2 latency.

Microbiology spectrum·2026
Same author

Efficient Method for High-Throughput Screening of Compound Libraries Targeting Human PD-L1.

ACS omega·2026
Same author

Modeling <i>cis</i>-regulatory variation in human brain enhancers across a large Parkinson's Disease cohort.

bioRxiv : the preprint server for biology·2026
Same author

Dosimetric evaluation of titanium and carbon spinal fixation systems in radiotherapy: Comparison of two dose calculation algorithms.

Medical dosimetry : official journal of the American Association of Medical Dosimetrists·2026
Same author

Steroidal A/B-ring fusion as a strategy for isoform-selective inhibition of human carbonic anhydrases.

RSC advances·2026
Same author

Primate lineage specification requires suppression of Alu hyperediting.

bioRxiv : the preprint server for biology·2026

Related Experiment Video

Updated: Apr 5, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K

Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif.

Petr Tesina1,2,3, Kateřina Čermáková4, Magdalena Hořejší3

  • 1Institute of Organic Chemistry and Biochemistry of the ASCR, v.v.i., Flemingovo nam. 2, 166 10 Prague, Czech Republic.

Nature Communications
|August 7, 2015
PubMed
Summary

Lens epithelium-derived growth factor (LEDGF/p75) is crucial for HIV integration and certain leukemias. Its interactions with other proteins, including HIV integrase, share similar binding modes, posing challenges for developing targeted therapies.

More Related Videos

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
07:03

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions

Published on: December 23, 2022

3.8K
In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

6.4K

Related Experiment Videos

Last Updated: Apr 5, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K
Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
07:03

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions

Published on: December 23, 2022

3.8K
In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

6.4K

Area of Science:

  • Molecular biology
  • Structural biology
  • Epigenetics

Background:

  • Lens epithelium-derived growth factor (LEDGF/p75) is an epigenetic reader and therapeutic target.
  • It plays a role in HIV integration and mixed lineage leukemia (MLL1) fusion-driven leukemia.
  • LEDGF/p75 interacts with various proteins via its integrase binding domain (IBD).

Purpose of the Study:

  • To structurally characterize LEDGF/p75 interactions with JPO2 and PogZ.
  • To identify novel LEDGF/p75 binding partners.
  • To understand how HIV integrase displaces cellular partners from LEDGF/p75.

Main Methods:

  • Structural characterization of protein-protein interactions.
  • Identification of intrinsically disordered binding motifs.
  • Validation of novel protein interactions.

Main Results:

  • Structural characterization of IBD interactions with JPO2 and PogZ.
  • The PogZ interaction is similar to the LEDGF/p75-MLL1 interaction.
  • An intrinsically disordered IBD-binding motif (IBM) is common to LEDGF/p75 partners.
  • IWS1 identified as a novel LEDGF/p75 partner.
  • HIV integrase displaces cellular partners from LEDGF/p75 through efficient binding.

Conclusions:

  • The conserved binding mode of LEDGF/p75 partners presents a challenge for developing selective inhibitors.
  • Understanding these interactions is key for therapeutic development against HIV and leukemia.