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

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

You might also read

Related Articles

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

Sort by
Same author

Impact of red blood cell rigidity on in vivo flow dynamics and lingering in bifurcations.

Biophysical journal·2026
Same author

Hyaluronic Acid-Functionalized Highly Porous Polymeric Materials for Stem Cell Culture.

Chemistry of materials : a publication of the American Chemical Society·2025
Same author

Tafazzin regulates neutrophil maturation and inflammatory response.

EMBO reports·2025
Same author

Correction to: Neutrophils cultured ex vivo from CD34 + stem cells are immature and genetically tractable.

Journal of translational medicine·2024
Same author

Modulation of Antioxidant Enzyme Expression of In Vitro Culture-Derived Reticulocytes.

Antioxidants (Basel, Switzerland)·2024
Same author

Deletions in the MAL gene result in loss of Mal protein, defining the rare inherited AnWj-negative blood group phenotype.

Blood·2024
Same journal

Compound heterozygous variants in F7 gene causing severe factor VII deficiency without bleeding: A genotypic and laboratory analysis.

Blood cells, molecules & diseases·2026
Same journal

Propofol attenuates H<sub>2</sub>O<sub>2</sub>-induced senescence in human umbilical vein endothelial cells by activating the NRF2/HO-1 axis.

Blood cells, molecules & diseases·2026
Same journal

Is it time to implement a hemorheology passport in sickle cell disease?

Blood cells, molecules & diseases·2026
Same journal

From blood viscosity to a hemorheology passport: Making sickle-cell monitoring clinically actionable.

Blood cells, molecules & diseases·2026
Same journal

A real-world analysis of polycythemia vera at two comprehensive cancer centers in Cali, Colombia.

Blood cells, molecules & diseases·2026
Same journal

Sickle Cell Disease: Can genetic variability influence pregnancy outcomes?

Blood cells, molecules & diseases·2026
See all related articles

Related Experiment Video

Updated: Jun 25, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Protein 4.2: a complex linker.

Timothy J Satchwell1, Debbie K Shoemark, Richard B Sessions

  • 1University of Bristol, Department of Biochemistry, School of Medical Sciences, University Walk, Bristol, BS8 1TD, UK.

Blood Cells, Molecules & Diseases
|March 10, 2009
PubMed
Summary
This summary is machine-generated.

Protein 4.2 is crucial for red blood cell membrane stability, linking key protein complexes. Its deficiency causes hereditary spherocytosis, highlighting its importance despite being understudied.

More Related Videos

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Related Experiment Videos

Last Updated: Jun 25, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
09:35

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

Area of Science:

  • Hematology
  • Molecular Biology
  • Cell Biology

Background:

  • Protein 4.2 is a major peripheral membrane protein in erythrocytes.
  • It plays a vital role in maintaining red blood cell membrane structure and stability.
  • Absence of protein 4.2 leads to hereditary spherocytosis.

Purpose of the Study:

  • To review current knowledge on protein 4.2.
  • To discuss its interactions and the implications of its deficiency.
  • To propose a novel homology structure for protein 4.2.

Main Methods:

  • Literature review of protein 4.2.
  • Analysis of protein interactions (band 3, CD47, ankyrin).
  • Homology modeling based on transglutaminase proteins.

Main Results:

  • Protein 4.2 connects band 3 and Rhesus protein complexes.
  • Deficiency severely impacts erythrocyte membrane stability.
  • A speculative "open" homology structure is proposed.

Conclusions:

  • Protein 4.2 is essential for erythrocyte membrane integrity.
  • Understanding its structure and interactions is key.
  • Further research may elucidate its precise function and therapeutic potential.