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

Conserved Binding Sites01:49

Conserved Binding Sites

5.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.2K
Conserved Binding Sites01:49

Conserved Binding Sites

2.0K
2.0K
Ligand Binding Sites02:40

Ligand Binding Sites

15.1K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.1K
Ligand Binding Sites02:40

Ligand Binding Sites

8.8K
8.8K
Nuclear Binding Energy02:13

Nuclear Binding Energy

14.8K
The difference between the calculated and experimentally measured masses is known as the mass defect of the atom. In the case of helium-4, the mass defect indicates a “loss” in mass of 4.0331 amu – 4.0026 amu = 0.0305 amu. The loss in mass accompanying the formation of an atom from protons, neutrons, and electrons is due to the conversion of that mass into energy that is evolved as the atom forms. The nuclear binding energy is the energy produced when the atoms’ nucleons are bound...
14.8K
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

7.4K
Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...
7.4K

You might also read

Related Articles

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

Sort by
Same author

Cycloparaphenylene-Derived Porous Organic Cylinders.

Journal of the American Chemical Society·2026
Same author

Self-Powered Smart Textiles for Accelerated Wound Healing through Band Alignment in Piezoelectric Heterojunctions.

ACS nano·2026
Same author

pH-responsive CDs-based nanoplatform for chemo-resistant esophageal cancer treatment via downregulation of HIF-1α related pathway.

Journal of nanobiotechnology·2026
Same author

De Novo developing nanoplatform encapsuling α-arbutin and α-syn inhibitor for precise treatment of Parkinson's disease.

Colloids and surfaces. B, Biointerfaces·2026
Same author

Hypoxia-Responsive Artificial Urinary Biomarker Probe for Early Detection of Drug-Induced Acute Kidney Injury.

Analytical chemistry·2026
Same author

ATG9B regulates mitochondrial integrity and apoptotic tumor cell death.

Molecular biology of the cell·2026

Related Experiment Video

Updated: Feb 5, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

7.1K

Macroautophagy Regulates Nuclear NOTCH1 Activity Through Multiple p62 Binding Sites.

Ting Zhang1, Lixia Guo1, Yuanyuan Wang1,2

  • 1Thoracic Disease Research Unit, Division of Pulmonary and Critical Care Medicine, College of Medicine and Science, Mayo Clinic, MN, USA.

IUBMB Life
|September 13, 2018
PubMed
Summary

Autophagy degrades NOTCH1 via p62 binding to its intracellular domain (NICD1). This process uniquely controls nuclear NICD1 activity, offering potential therapeutic targets for NOTCH1-related diseases.

Keywords:
NOTCH1autophagydegradationp62

More Related Videos

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins
12:24

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

Published on: July 2, 2010

54.2K
Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry
11:39

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry

Published on: July 21, 2017

32.3K

Related Experiment Videos

Last Updated: Feb 5, 2026

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

7.1K
PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins
12:24

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

Published on: July 2, 2010

54.2K
Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry
11:39

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry

Published on: July 21, 2017

32.3K

Area of Science:

  • Cellular biology
  • Molecular mechanisms of protein degradation

Background:

  • NOTCH1 signaling is crucial for development and disease.
  • NOTCH1 activation involves proteolytic cleavage releasing the intracellular domain (NICD1).
  • Autophagy's role in NOTCH1 degradation is known, but mechanisms are unclear.

Purpose of the Study:

  • To elucidate the mechanism by which autophagy degrades NOTCH1.
  • To investigate the role of p62 and LC3 in NOTCH1 degradation.
  • To determine the impact of autophagy on nuclear NICD1 activity.

Main Methods:

  • Investigated p62-dependent binding between NICD1 and LC3.
  • Utilized domain deletion mutants of NICD1.
  • Assessed NICD1 localization and transcriptional activity under varying autophagy conditions.

Main Results:

  • Autophagy promotes NOTCH1 degradation through p62-dependent binding to LC3.
  • p62 binds to multiple sites on NICD1, facilitating its degradation.
  • Autophagy inhibition leads to NICD1 accumulation in cytoplasm and nucleus, enhancing its transcriptional activity.
  • Autophagy's regulation of nuclear NICD1 is specific to NICD1.

Conclusions:

  • Autophagy tightly regulates nuclear NOTCH1 activity via multiple p62 binding sites.
  • Modulating autophagy presents a potential therapeutic strategy for NOTCH1-related diseases.