Jove
Visualize
Contáctanos

Videos de Conceptos Relacionados

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.Fatty acids tails of phospholipids can be either saturated or...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

Synthesis, Properties, and Electrochemical Proton Reduction of a Homoleptic Tetrathiolato Ni-Site Model of [NiFe]-Hydrogenase.

Inorganic chemistry·2025
Same author

Nucleotide- and metalloid-driven conformational changes in the arsenite efflux ATPase ArsA.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

The zinc metalloprotein MigC impacts cell wall biogenesis through interactions with an essential Mur ligase in Acinetobacter baumannii.

PLoS pathogens·2025
Same author

Quantum dot-based thermometry uncovers decreased myosin efficiency in an experimental intensive care unit model.

Frontiers in physiology·2024
Same author

Fpa (YlaN) is an iron(II) binding protein that functions to relieve Fur-mediated repression of gene expression in <i>Staphylococcus aureus</i>.

mBio·2024
Same author

ATH434, a promising iron-targeting compound for treating iron regulation disorders.

Metallomics : integrated biometal science·2024
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

Video Experimental Relacionado

Updated: Jun 14, 2026

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

Los lípidos de membrana influyen en el complejo proteico ensamblaje-desensamblaje.

Leah Shin1, Won Jin Cho, Jeremy D Cook

  • 1Department of Physiology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.

Journal of the American Chemical Society
|April 9, 2010
PubMed
Resumen
Este resumen es generado por máquina.

Las vesículas asociadas al colesterol producen complejos de anillos t-/v-SNARE más pequeños en comparación con las vesículas de L-alfa-lisofosfatidilcolina (LPC). LPC también promueve el factor sensible a la N-etilmaleimida + el desmontaje inducido por trifosfato de adenosina de las estructuras de la hoja beta en estos complejos.

Más Videos Relacionados

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
10:31

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

Published on: September 2, 2020

Videos de Experimentos Relacionados

Last Updated: Jun 14, 2026

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
10:31

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

Published on: September 2, 2020

Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Biología Molecular Biología Molecular
  • La biofísica es la biofísica.

Sus antecedentes:

  • Los receptores de proteínas de adherencia NSF solubles (SNAREs) median la fusión de la membrana, un proceso crítico en el transporte celular.
  • Los mecanismos estructurales precisos y las interacciones lipídicas que rigen el montaje y desmontaje del complejo SNARE siguen siendo incompletamente entendidos.
  • Comprender las dinámicas complejas de SNARE es crucial para descifrar las vías de tráfico intracelular.

Objetivo del estudio:

  • Investigar la influencia de diferentes lípidos, específicamente el colesterol y la L-alfa-lisofosfatidilcolina (LPC), en las propiedades estructurales de los complejos t-/v-SNARE.
  • Aclarar el papel del factor sensible a la N-etilmaleimida (NSF) y el trifosfato de adenosina (ATP) en la modulación de la estructura del complejo SNARE en presencia de distintos entornos lipídicos.

Principales métodos:

  • Se empleó microscopía de fuerza atómica (AFM) para medir el tamaño de los complejos de anillos t-/v-SNARE formados con vesículas asociadas al colesterol versus vesículas que contienen LPC.
  • Se utilizó la espectroscopia de dicroísmo circular (CD) para analizar los cambios estructurales secundarios (contenido beta-sheet y alfa-helical) dentro de los complejos t-/v-SNARE en diferentes condiciones.

Principales resultados:

  • Los complejos de anillos t-/v-SNARE formados con vesículas asociadas al colesterol eran aproximadamente un 11% más pequeños que los formados con vesículas que contienen LPC.
  • La espectroscopia de CD reveló que en presencia de LPC, NSF + ATP indujo un desmontaje significativo de las estructuras de la hoja beta dentro del complejo t-/v-SNARE.
  • El contenido alfa-hélico del complejo t-/v-SNARE se mantuvo en gran medida no afectado por NSF + ATP en presencia de LPC.

Conclusiones:

  • El colesterol y el LPC regulan diferencialmente el tamaño y la integridad estructural de los complejos t-/v-SNARE.
  • LPC, junto con NSF y ATP, facilita la ruptura de las estructuras secundarias de la hoja beta en los complejos SNARE, lo que sugiere un mecanismo mediado por lípidos para el desmontaje de SNARE.
  • Estos hallazgos resaltan la importancia del microambiente lipídico en el control de la función del complejo SNARE y la regulación de la fusión de la membrana.