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

Amyloid Fibrils03:03

Amyloid Fibrils

11.9K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
11.9K
Amyloid Fibrils03:03

Amyloid Fibrils

6.4K
6.4K
Alternative RNA Splicing02:18

Alternative RNA Splicing

25.2K
Alternative RNA splicing is the regulated splicing of exons and introns to produce different mature mRNAs from a single pre-mRNA. Unlike in constitutive splicing where a single gene produces a single type of mRNA, alternative splicing allows an organism to produce multiple proteins from a single gene and plays an important role in protein diversity.
There are five types of alternative RNA splicing that vary in the ways the pre-mRNA segments are removed or retained in the mature mRNA. The first...
25.2K
RNA Editing02:23

RNA Editing

9.9K
RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...
9.9K
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

32.8K
Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
32.8K
Eukaryotic RNA Polymerases00:58

Eukaryotic RNA Polymerases

27.1K
RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...
27.1K

You might also read

Related Articles

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

Sort by
Same author

Chemoradiation (CCRT) Effects on Head and Neck Muscles: Insights Into CCRT-Induced Dysphagia.

The Laryngoscope·2026
Same author

Physical interactions within the SIR heterochromatin complex potentiate inter-subunit communication and gene repression.

Cell reports·2026
Same author

A mutation in the nuclear speckle and splicing factor SRRM2 is associated with multisystem proteinopathy and causes dysregulation of synapse-associated genes.

RNA (New York, N.Y.)·2026
Same author

The assembly of stress granules during foot-and-mouth disease virus infection is uncoupled from activation of cellular intrinsic antiviral signalling.

PLoS pathogens·2026
Same author

TDP-43 Sustains Satellite Cells to Maintain and Regenerate Skeletal Muscle.

bioRxiv : the preprint server for biology·2026
Same author

Alphaviral non-structural protein-host RBP co-condensation as a mechanism to sustain virus replication.

Molecular cell·2026

Related Experiment Video

Updated: Feb 2, 2026

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy
07:07

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy

Published on: August 3, 2021

3.2K

TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle.

Thomas O Vogler1,2, Joshua R Wheeler2,3, Eric D Nguyen2,4

  • 1Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO, USA.

Nature
|November 23, 2018
PubMed
Summary

Cytoplasmic aggregates of TDP-43 protein are common in neuromuscular diseases. Researchers discovered that normal muscle regeneration involves TDP-43 forming temporary "myo-granules," which may lead to disease aggregates if not cleared.

More Related Videos

Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae
07:14

Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae

Published on: February 25, 2022

6.6K
Myo-mechanical Analysis of Isolated Skeletal Muscle
08:42

Myo-mechanical Analysis of Isolated Skeletal Muscle

Published on: February 22, 2011

27.6K

Related Experiment Videos

Last Updated: Feb 2, 2026

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy
07:07

Measuring Glucose Uptake in Drosophila Models of TDP-43 Proteinopathy

Published on: August 3, 2021

3.2K
Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae
07:14

Optogenetic Phase Transition of TDP-43 in Spinal Motor Neurons of Zebrafish Larvae

Published on: February 25, 2022

6.6K
Myo-mechanical Analysis of Isolated Skeletal Muscle
08:42

Myo-mechanical Analysis of Isolated Skeletal Muscle

Published on: February 22, 2011

27.6K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Cytoplasmic aggregation of TDP-43 is a hallmark of neuromuscular diseases like ALS and inclusion body myopathy.
  • While TARDBP mutations cause some TDP-43 aggregation, most patients have wild-type TDP-43 aggregates, suggesting an unknown mechanism.

Purpose of the Study:

  • To investigate the mechanism behind wild-type TDP-43 aggregation in neuromuscular diseases.
  • To explore the normal function of TDP-43 in skeletal muscle and its potential role in disease pathogenesis.

Main Methods:

  • Studied TDP-43's role in skeletal muscle regeneration in mouse and human models.
  • Characterized TDP-43-containing cytoplasmic assemblies (myo-granules).
  • Assessed myo-granule formation, mRNA binding, clearance, and potential for seeding amyloid fibrils.

Main Results:

  • TDP-43 is essential for skeletal muscle formation and forms transient, amyloid-like "myo-granules" during regeneration.
  • These myo-granules bind mRNAs for sarcomeric proteins and are cleared as muscle matures.
  • Myo-granules can seed TDP-43 amyloid fibrils in vitro and are elevated in an inclusion body myopathy mouse model.

Conclusions:

  • Myo-granules represent a normal, transient assembly of TDP-43 during muscle regeneration.
  • Dysregulation in myo-granule assembly or clearance may be a primary source of toxic TDP-43 aggregates in common neuromuscular diseases.