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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

19.5K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.5K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

2.8K
2.8K
Termination of Translation01:44

Termination of Translation

27.7K
The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
27.7K
Termination of Translation01:44

Termination of Translation

6.8K
6.8K
Extrinsic and Intrinsic Pathways of Hemostasis01:20

Extrinsic and Intrinsic Pathways of Hemostasis

12.7K
Blood clotting or coagulation involves extrinsic and intrinsic pathways, which ultimately merge into the common pathway, forming a fibrin clot.
The Extrinsic Pathway
The extrinsic pathway of coagulation is typically initiated by tissue damage that exposes blood to tissue factor (TF), a protein released by the damaged tissue cells outside the blood vessels—this interaction with TF triggers biochemical reactions involving specific clotting factors. The key player here is Factor VII, which...
12.7K
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

8.5K
Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
8.5K

You might also read

Related Articles

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

Sort by
Same author

Non-Classical Binding Mechanisms of Ferrocene-Modified Imatinib and Nilotinib Analogues in BCR-ABL1 Kinase Revealed by Computational Analysis.

Molecules (Basel, Switzerland)·2026
Same author

Extensive conformational and physical plasticity protects HER2-HER3 tumorigenic signaling.

Cell reports·2026
Same author

Ligand trapping as a key mechanism governing drug residence time, binding affinity, and potency.

Drug discovery today·2026
Same author

Metabolic alterations driven by PFKFB3 upregulation confer resistance to trastuzumab in HER2-positive breast cancer.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2026
Same author

FNA biopsy of breast specimens effectively harvests cells for patient-derived organoids modeling ductal carcinoma in situ.

Cancer cytopathology·2025
Same author

ADCC: the rock band led by therapeutic antibodies, tumor and immune cells.

Frontiers in immunology·2025

Related Experiment Video

Updated: Feb 4, 2026

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
05:13

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Published on: January 12, 2024

1.5K

A Dimerization Function in the Intrinsically Disordered N-Terminal Region of Src.

Danislav S Spassov1, Ana Ruiz-Saenz1, Amit Piple1

  • 1Department of Medicine, Helen Diller Family Comprehensive Cancer Center, University of California, San Francisco, San Francisco, CA 94143, USA.

Cell Reports
|October 11, 2018
PubMed
Summary

The Src kinase N-terminal region binds a dimerization partner, enhancing its activity. This dimerization and phosphorylation form a bistable switch, positioning the N-terminal region as a key signaling hub.

Keywords:
Srcdimerdimerizationintrinsically disordered proteinkinase domainmyristoyltyrosine 416tyrosine 419unique domain

More Related Videos

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.4K

Related Experiment Videos

Last Updated: Feb 4, 2026

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
05:13

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Published on: January 12, 2024

1.5K
Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

2.3K
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
12:47

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins

Published on: December 27, 2016

19.4K

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein Kinase Regulation

Background:

  • Src kinases are crucial regulators of cellular processes.
  • While structured domains are well-understood, the role of the intrinsically disordered N-terminal region remains unclear.
  • Understanding Src kinase regulation is vital for deciphering complex cellular signaling.

Purpose of the Study:

  • To elucidate the function of the intrinsically disordered N-terminal region of Src kinases.
  • To investigate the role of dimerization in Src kinase regulation and activity.
  • To identify the N-terminal region as a potential signaling hub.

Main Methods:

  • Crystallographic studies to identify protein-protein interactions.
  • Biochemical assays to assess autophosphorylation and substrate phosphorylation.
  • Analysis of dimerization-dependent and independent Src kinase activity.

Main Results:

  • The N-terminal region binds a dimerization partner within a hydrophobic pocket in the kinase domain.
  • Dimerization significantly enhances Src autophosphorylation and substrate phosphorylation.
  • Dimerization and Y419 phosphorylation act as codependent events, forming a bistable switch.

Conclusions:

  • The N-terminal region functions as a critical dimerization interface.
  • Dimerization mediated by the N-terminal region is essential for full Src kinase activation.
  • The N-terminal region acts as a central signaling hub, regulating Src family kinase activities and functions.