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

Anaphase Promoting Complex00:50

Anaphase Promoting Complex

3.0K
The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
3.0K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.0K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.0K
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

3.3K
The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
3.3K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.5K
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.5K
Separation of Sister Chromatids02:17

Separation of Sister Chromatids

3.8K
At the transition from prophase to metaphase, there is a reduction in cohesion along the chromosomal arms, resulting in the resolution of sister chromatids. However, residual cohesin connections remain to hold the sister chromatids together until the transition from metaphase to anaphase. The residual connection prevents any premature separation of sister chromatids, blocking the risks of aneuploidy within the daughter cells.
At the onset of anaphase, separase, a proteolytic enzyme, is...
3.8K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.2K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.2K

You might also read

Related Articles

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

Sort by
Same author

Alternative Polyadenylation Signatures Distinguish Maladaptive Right Ventricular Remodeling in Pulmonary Hypertension: Implications for RNA-Based Diagnostics and Therapeutics.

British journal of biomedical science·2026
Same author

The UTHealth Houston Adult Cardiovascular Genomics Certificate Program: Efficacy and Impact on Healthcare Professionals.

Research square·2024
Same author

Hairpin-like siRNA-Based Spherical Nucleic Acids.

Journal of the American Chemical Society·2022
Same author

Dual-Readout Sandwich Immunoassay for Device-Free and Highly Sensitive Anthrax Biomarker Detection.

Analytical chemistry·2020
Same author

Identification and characterization of self-association domains on small ankyrin 1 isoforms.

Journal of molecular and cellular cardiology·2020
Same author

The effector mechanism of siRNA spherical nucleic acids.

Proceedings of the National Academy of Sciences of the United States of America·2020

Related Experiment Video

Updated: Sep 26, 2025

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments
06:53

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments

Published on: February 12, 2021

5.2K

Obscurin regulates ankyrin macromolecular complex formation.

Janani Subramaniam1, Gokay Yamankurt1, Shane R Cunha1

  • 1Department of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, Houston, TX 77030, United States of America.

Journal of Molecular and Cellular Cardiology
|April 21, 2022
PubMed
Summary

Obscurin, a muscle scaffolding protein, binds two distinct ankyrins (small ankyrin 1.5 and ankyrin-G 107) independently. This interaction targets these ankyrins to the cardiomyocyte M-line, revealing a novel scaffolding mechanism.

Keywords:
Alternative splicingAnkG107AnkyrinObscurinsAnk1.5

More Related Videos

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Published on: December 10, 2015

7.5K
Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
11:50

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

2.2K

Related Experiment Videos

Last Updated: Sep 26, 2025

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments
06:53

Use of Primary Cultured Hippocampal Neurons to Study the Assembly of Axon Initial Segments

Published on: February 12, 2021

5.2K
Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

Published on: December 10, 2015

7.5K
Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
11:50

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

Published on: June 23, 2022

2.2K

Area of Science:

  • Muscle biology
  • Cellular and molecular biology
  • Protein interactions

Background:

  • Obscurin is a key scaffolding protein in striated muscle, crucial for sarcolemmal integrity and the organization of the sarcoplasmic reticulum.
  • Ankyrins are adaptor proteins known to interact with obscurin, but the specifics of interactions with multiple ankyrin isoforms are not fully understood.
  • Previous research has focused on obscurin's interaction with individual ankyrin proteins.

Purpose of the Study:

  • To investigate the interaction between obscurin and two specific ankyrins: small ankyrin 1.5 (sAnk1.5) and the muscle-specific ankyrin-G 107 (AnkG107).
  • To elucidate the mechanism by which obscurin bridges these two ankyrins and its role in targeting them to the sarcomeric M-line.
  • To characterize the binding domains involved and the functional consequences of these interactions.

Main Methods:

  • In vitro binding assays and co-precipitation assays were used to confirm protein interactions.
  • Förster resonance energy transfer (FRET) analysis, specifically Fluorescence Loss In-Inducing Mutation (FLIM-FRET), was employed to study proximity and interaction dynamics.
  • Mutagenesis of obscurin's ankyrin-binding domains (ABDs) and analysis of ankyrin localization in cardiomyocytes were performed.

Main Results:

  • Obscurin interacts with both sAnk1.5 and AnkG107 via independent ABDs at its carboxyl terminus.
  • Obscurin acts as a bridge connecting sAnk1.5 and AnkG107, even without direct interaction between the two ankyrins.
  • AnkG107 recruits β-spectrin, and mutations in obscurin's ABDs disrupt complex formation and M-line localization of ankyrin constructs.

Conclusions:

  • Obscurin utilizes distinct binding domains to interact with two different ankyrin complexes (sAnk1.5 and AnkG107).
  • This interaction mechanism is essential for targeting these ankyrin complexes to the sarcomeric M-line in ventricular cardiomyocytes.
  • The findings support a model where obscurin plays a critical role in organizing sarcomeric structure by anchoring multiple protein complexes.