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

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

7.5K
Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
7.5K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
2.6K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

7.3K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
7.3K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.2K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.2K
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

8.2K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
8.2K
Rab Proteins01:14

Rab Proteins

4.0K
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...
4.0K

You might also read

Related Articles

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

Sort by
Same author

Strategic Applications of Single-Atom Skeletal Editing in Natural Product Synthesis.

Journal of the American Chemical Society·2026
Same author

Seven-Step Total Synthesis of Conidiogenone B Enabled by Radical Cyclizations.

Journal of the American Chemical Society·2026
Same author

Light-Regulated Agonists Spatiotemporally Activating the Vitamin D Receptor Mitigate Psoriasis-like Inflammation in Mice without Inducing Hypercalcemia.

ACS central science·2025
Same author

Comparative analysis of complanadine A total syntheses.

Beilstein journal of organic chemistry·2025
Same author

Total Synthesis of (-)-Psathyrin A Enabled by Radical Cyclization.

Journal of the American Chemical Society·2025
Same author

Reverse polarity of amide nitrogen enables expedient access to N-cyano amides.

Nature communications·2025
Same journal

Targeting developmental reprogramming: hPSC insights for cancer interception.

Trends in pharmacological sciences·2026
Same journal

July 2026 issue first authors.

Trends in pharmacological sciences·2026
Same journal

Chronobiomaterials for circadian-aligned brain therapeutics.

Trends in pharmacological sciences·2026
Same journal

Biosensors for translatable GPCR bias.

Trends in pharmacological sciences·2026
Same journal

ECM stiffness and epigenetics in organ fibrosis.

Trends in pharmacological sciences·2026
Same journal

Which HTT transcript to lower?

Trends in pharmacological sciences·2026
See all related articles

Related Experiment Video

Updated: Aug 13, 2025

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

3.6K

Taming PRMT5-adaptor protein interactions.

Hunter S Sims1, Mingji Dai2

  • 1Department of Chemistry, Emory University, Atlanta, GA 30322, USA; Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.

Trends in Pharmacological Sciences
|January 20, 2023
PubMed
Summary
This summary is machine-generated.

New stapled peptides inhibit Protein Arginine Methyltransferase (PRMT) 5, a key epigenetic regulator. This discovery offers novel therapeutic strategies by selectively targeting PRMT5 interactions for disease treatment.

Keywords:
Rio domain-containing protein (RioK1)chloride channel nucleotide sensitive protein 1A (pICln)protein arginine methyltransferase 5 (PRMT5)protein-protein interaction (PPI) inhibitorsolid-phase peptide synthesis (SPPS)stapled peptide

More Related Videos

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
08:11

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Published on: August 7, 2021

4.2K
Novel RNA-Binding Proteins Isolation by the RaPID Methodology
11:19

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Published on: September 30, 2016

9.1K

Related Experiment Videos

Last Updated: Aug 13, 2025

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

3.6K
Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
08:11

Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

Published on: August 7, 2021

4.2K
Novel RNA-Binding Proteins Isolation by the RaPID Methodology
11:19

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Published on: September 30, 2016

9.1K

Area of Science:

  • Epigenetics
  • Molecular Biology
  • Drug Discovery

Background:

  • Protein Arginine Methyltransferase (PRMT) 5 is a crucial epigenetic regulator implicated in various diseases.
  • PRMT5's role in disease pathogenesis makes it a significant therapeutic target.
  • Understanding PRMT5 interactions is key to developing targeted therapies.

Purpose of the Study:

  • To identify novel inhibitors of Protein Arginine Methyltransferase (PRMT) 5.
  • To explore the therapeutic potential of modulating PRMT5 activity.
  • To investigate the inhibition of PRMT5 interactions with its adaptor proteins.

Main Methods:

  • Design and synthesis of stapled peptides.
  • Biochemical assays to assess PRMT5 inhibition.
  • Analysis of PRMT5-adaptor protein interactions.

Main Results:

  • Identification of stapled peptides that effectively inhibit PRMT5.
  • Demonstration that these peptides disrupt PRMT5 interactions with specific adaptor proteins.
  • Validation of selective PRMT5 modulation through peptide-based inhibition.

Conclusions:

  • Stapled peptides represent a promising new class of PRMT5 inhibitors.
  • Selective modulation of PRMT5 activity is achievable through peptide-based therapeutics.
  • This research opens avenues for novel epigenetic therapies targeting PRMT5.