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

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.1K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K
Cross-bridge Cycle01:26

Cross-bridge Cycle

116.9K
As muscle contracts, the overlap between the thin and thick filaments increases, decreasing the length of the sarcomere—the contractile unit of the muscle—using energy in the form of ATP. At the molecular level, this is a cyclic, multistep process that involves binding and hydrolysis of ATP, and movement of actin by myosin.
116.9K
Muscle Contraction01:10

Muscle Contraction

6.2K
In skeletal muscles, acetylcholine is released by nerve terminals at the motor endplate—the point of synaptic communication between motor neurons and muscle fibers. The binding of acetylcholine to its receptors on the sarcolemma allows entry of sodium ions into the cell and triggers an action potential in the muscle cell. Thus, electrical signals from the brain are transmitted to the muscle. Subsequently, the enzyme acetylcholinesterase breaks down acetylcholine to prevent excessive...
6.2K
Smooth Muscle Contraction01:25

Smooth Muscle Contraction

2.5K
Smooth muscle contraction is a complex process vital for various bodily functions, from maintaining blood vessel tension to facilitating the movement of food through the digestive tract. Unlike striated muscles, smooth muscle contraction begins more slowly and lasts longer.
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...
2.5K
Relaxation of Skeletal Muscles01:29

Relaxation of Skeletal Muscles

3.0K
The period of muscle contraction primarily influences the duration of stimulation at the neuromuscular junction (NMJ), the presence of free calcium ions in the sarcoplasm, and the availability of energy or ATP to support contractions.
When an action potential reaches the axon terminal, it depolarizes the membrane and opens voltage-gated sodium channels. Sodium ions enter the cell, further depolarizing the presynaptic membrane. This depolarization causes voltage-gated calcium channels to open....
3.0K
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

8.9K
Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
8.9K

You might also read

Related Articles

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

Sort by
Same author

Association of athlete's heart and ACE I/D genotype with later-life left ventricular hypertrophy: a retrospective cohort study.

BMC cardiovascular disorders·2026
Same author

An immune-associated mitochondrial DNA variant with sex differences reveals a putative novel microprotein called MASL.

Immunity & ageing : I & A·2026
Same author

Collagen Type V alpha 1 chain and alpha-actinin-3 variants predict knee ligament injury risk in professional football players.

Journal of experimental orthopaedics·2026
Same author

Impact of pre-vaccination active vitamin D levels on COVID-19 mRNA vaccine-induced immunity in a Japanese cohort.

Vaccine·2026
Same author

Association of the ACTN3 Genotype with Muscle Function: A Systematic Review and Meta-analysis.

International journal of sports medicine·2026
Same author

RAB3GAP2 is a regulator of skeletal muscle endothelial cell proliferation and associated with capillary-to-fiber ratio.

Cell reports·2026

Related Experiment Video

Updated: Jun 7, 2025

Isolation of Human Myoblasts, Assessment of Myogenic Differentiation, and Store-operated Calcium Entry Measurement
10:45

Isolation of Human Myoblasts, Assessment of Myogenic Differentiation, and Store-operated Calcium Entry Measurement

Published on: July 26, 2017

10.0K

MOTS-c modulates skeletal muscle function by directly binding and activating CK2.

Hiroshi Kumagai1, Su-Jeong Kim1, Brendan Miller1

  • 1The Leonard Davis School of Gerontology, University of Southern California, Los Angeles, CA, USA.

Iscience
|November 19, 2024
PubMed
Summary
This summary is machine-generated.

Mitochondrial microprotein MOTS-c activates protein kinase CK2, improving metabolism and preventing muscle atrophy. This interaction is crucial for MOTS-c

Keywords:
Physiologycell biology

More Related Videos

Application of Chronic Stimulation to Study Contractile Activity-induced Rat Skeletal Muscle Phenotypic Adaptations
09:50

Application of Chronic Stimulation to Study Contractile Activity-induced Rat Skeletal Muscle Phenotypic Adaptations

Published on: January 25, 2018

6.7K
Myo-mechanical Analysis of Isolated Skeletal Muscle
08:42

Myo-mechanical Analysis of Isolated Skeletal Muscle

Published on: February 22, 2011

26.8K

Related Experiment Videos

Last Updated: Jun 7, 2025

Isolation of Human Myoblasts, Assessment of Myogenic Differentiation, and Store-operated Calcium Entry Measurement
10:45

Isolation of Human Myoblasts, Assessment of Myogenic Differentiation, and Store-operated Calcium Entry Measurement

Published on: July 26, 2017

10.0K
Application of Chronic Stimulation to Study Contractile Activity-induced Rat Skeletal Muscle Phenotypic Adaptations
09:50

Application of Chronic Stimulation to Study Contractile Activity-induced Rat Skeletal Muscle Phenotypic Adaptations

Published on: January 25, 2018

6.7K
Myo-mechanical Analysis of Isolated Skeletal Muscle
08:42

Myo-mechanical Analysis of Isolated Skeletal Muscle

Published on: February 22, 2011

26.8K

Area of Science:

  • Mitochondrial biology
  • Metabolic regulation
  • Molecular mechanisms of aging

Background:

  • Mitochondrial open reading frame of the 12S rRNA-c (MOTS-c) is a peptide hormone that regulates metabolism and combats age-related diseases.
  • The precise molecular targets and mechanisms underlying MOTS-c's beneficial effects remain incompletely understood.

Purpose of the Study:

  • To identify and functionally characterize the direct molecular targets of MOTS-c.
  • To elucidate the role of these targets in mediating MOTS-c's physiological effects on metabolism and muscle health.

Main Methods:

  • In vitro binding assays to assess MOTS-c interaction with candidate proteins.
  • Cell-free kinase assays to determine MOTS-c's effect on protein kinase activity.
  • In vivo studies using mouse models to evaluate the impact of MOTS-c administration and CK2 inhibition on skeletal muscle and glucose metabolism.
  • Analysis of tissue-specific effects and molecular interactions in fat and muscle tissues.
  • Investigation of a naturally occurring MOTS-c variant (K14Q MOTS-c) and its functional consequences.

Main Results:

  • MOTS-c directly binds to and activates the protein kinase CK2 (casein kinase 2).
  • MOTS-c administration in mice prevented skeletal muscle atrophy and enhanced glucose uptake, effects dependent on CK2 activity.
  • MOTS-c exhibited tissue-specific effects, activating CK2 in muscle but suppressing it in fat.
  • A naturally occurring variant, K14Q MOTS-c, showed reduced CK2 binding and lacked MOTS-c's physiological effects.
  • Male carriers of K14Q MOTS-c had increased risk for sarcopenia and type 2 diabetes (T2D), while females showed an age-specific reduced risk of T2D.

Conclusions:

  • Protein kinase CK2 is a direct and functional target required for the metabolic and anti-atrophy effects of MOTS-c.
  • Differential regulation of CK2 by MOTS-c in distinct tissues contributes to its tissue-specific actions.
  • Naturally occurring variants of MOTS-c with impaired CK2 interaction may influence susceptibility to metabolic disorders and sarcopenia.