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

The Sarcomere01:08

The Sarcomere

A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each myosin...
Microtubule Instability02:17

Microtubule Instability

Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well characterized.
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

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...

You might also read

Related Articles

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

Sort by
Same author

Corrigendum to "'Erythritol', a safe natural sweetener exhibits multi-stage anti-malarial activity by permeating into Plasmodium falciparum through aquaglyceroporin channel" [Biochem. Pharmacol. 205 (2022) 115287].

Biochemical pharmacology·2026
Same author

Red cell shape regulation by band 3-ankyrin-spectrin linkage: implications for clinical severity of bovine hereditary spherocytosis.

Blood. Red cells & iron·2026
Same author

The red blood cell proteome and interactome identify a Band 3-BLVRB axis regulating hypoxic metabolic adaptation.

Blood·2026
Same author

Stag2 dependent chromatin remodeling enforces the erythroid-specific Gata1 cistrome.

Blood·2026
Same author

Transcriptomic and metabolomic analyses reveal cobalt-induced mitochondrial metabolic alterations in human cortical organoids.

Toxicology·2026
Same author

RPS19 and RPL5 haploinsufficient models reveal divergent ribosomal subunit controls of fetal hematopoiesis.

Nature communications·2026

Related Experiment Video

Updated: Jul 19, 2026

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos
12:35

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Published on: April 14, 2023

Tropomyosin modulates erythrocyte membrane stability.

Xiuli An1, Marcela Salomao, Xinhua Guo

  • 1Red Cell Physiology Laboratory, New York Blood Center, New York, NY 10021, USA. xan@nybloodcenter.org

Blood
|September 30, 2006
PubMed
Summary

Tropomyosin (TM) stabilizes the spectrin-actin-4.1R complex in red blood cells, crucial for membrane mechanical stability. Removing TM impairs membrane function, highlighting TM's essential role in erythrocyte structural integrity.

More Related Videos

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells
08:24

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells

Published on: August 18, 2017

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
12:38

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

Related Experiment Videos

Last Updated: Jul 19, 2026

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos
12:35

Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos

Published on: April 14, 2023

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells
08:24

Nitrogen Cavitation and Differential Centrifugation Allows for Monitoring the Distribution of Peripheral Membrane Proteins in Cultured Cells

Published on: August 18, 2017

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
12:38

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

Area of Science:

  • Cell biology
  • Biochemistry
  • Biophysics

Background:

  • The erythrocyte membrane skeleton, a network of spectrin and actin, provides mechanical stability to red blood cells.
  • The spectrin-actin-4.1R complex forms critical nodes within this network, but the roles of associated proteins like tropomyosin (TM) are not fully understood.

Purpose of the Study:

  • To investigate the specific function of tropomyosin (TM) in maintaining the mechanical stability of the erythrocyte membrane.
  • To elucidate the mechanism by which TM contributes to the integrity of the spectrin-actin-4.1R junctional complex.

Main Methods:

  • Selective elimination of tropomyosin (TM) from red blood cell membranes (resealed ghosts).
  • Assessment of mechanical stability of TM-depleted membranes.
  • Analysis of beta-spectrin peptide binding to membrane junctions in situ to evaluate complex stability.
  • Testing the specificity of TM's stabilizing effect using endogenous versus muscle isoforms.

Main Results:

  • Red blood cell membranes lacking TM exhibited significantly impaired mechanical stability.
  • The destabilization of the spectrin-actin-4.1R complex was confirmed by facilitated beta-spectrin peptide entry into junctions.
  • Only the endogenous erythrocyte TM isoform, not muscle TM, could restore membrane mechanical stability, indicating high specificity.

Conclusions:

  • Tropomyosin (TM) plays a critical, specific role in enhancing the mechanical stability of erythrocyte membranes.
  • TM functions by stabilizing the spectrin-actin-4.1R junctional complex, thereby maintaining red blood cell structural integrity under mechanical stress.