Jove
Visualize
Contáctanos
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

Videos de Conceptos Relacionados

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
Cell Sorting During Development
Cell sorting plays an...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

A functional investigation of antibody Fc-FcRn variant binding guided by <i>in silico</i> free energy perturbation methods.

bioRxiv : the preprint server for biology·2026
Same author

Proteome-wide prediction of interactions between structured domains and peptide motifs reveals functionally coherent subnetworks.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Early clonal dominance at priming sets the trajectory for broad HIV serum neutralization.

bioRxiv : the preprint server for biology·2026
Same author

PrePPI - Structure-based Prediction of Protein-protein Interactomes and Networks.

Journal of molecular biology·2026
Same author

Genetic diversity of the malaria vaccine candidate PfRIPR in a high transmission region of Senegal.

iScience·2026
Same author

Env-antibody coevolution identifies B cell priming as the principal bottleneck to HIV V2 apex broadly neutralizing antibody development.

Science immunology·2026

Video Experimental Relacionado

Updated: May 7, 2026

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
10:05

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

11.7K

Estructuras de ectodominio de cadherina tipo II: implicaciones para la especificidad de la cadherina clásica.

Saurabh D Patel1, Carlo Ciatto, Chien Peter Chen

  • 1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

Cell
|March 28, 2006
PubMed
Resumen

Las cadherinas clásicas (tipo I y II) median la adhesión celular. El análisis estructural revela interfaces adhesivas únicas en las cadherinas de tipo II, impulsadas por cadenas beta intercambiadas y residuos de triptófano conservados, que dictan la especificidad celular.

Más Videos Relacionados

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.6K
Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

10.9K

Videos de Experimentos Relacionados

Last Updated: May 7, 2026

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
10:05

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

11.7K
Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.6K
Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

10.9K

Área de la Ciencia:

  • Biología celular Biología celular.
  • Biología estructural Biología estructural.
  • La bioquímica es la bioquímica.

Sus antecedentes:

  • Las cadherinas clásicas (tipo I y II) son moléculas de adhesión celular cruciales.
  • Sus dominios extracelulares determinan el reconocimiento y la especificidad célula-célula.

Objetivo del estudio:

  • Para aclarar la base estructural de la especificidad de la adhesión celular en las cadherinas clásicas de tipo II.
  • Para comparar las interfaces adhesivas de las cadherinas tipo I y tipo II.

Principales métodos:

  • Determinación de la estructura cristalina de regiones de ectodominio a partir de tres cadherinas de tipo II.
  • Análisis de las interfaces proteicas y de los residuos conservados.
  • Ensayos funcionales in vitro e in vivo con las cadherinas quiméricas.

Principales resultados:

  • Las cadherinas de tipo II forman dímeros adhesivos a través de cadenas beta N-terminales intercambiadas en sus dominios extracelulares de cadherina-1 (EC1).
  • Estas interfaces presentan dos residuos de triptófano conservados y regiones hidrofóbicas únicas, distintas de las cadherinas de tipo I.
  • Los dominios EC1 de las cadherinas de tipo I y tipo II dictan la especificidad adhesiva celular in vitro.
  • Los experimentos con cadherina quimérica demuestran que la identidad del dominio EC1 es crítica para la función de la cadherina tipo II en la segregación de las neuronas motoras in vivo.

Conclusiones:

  • El dominio EC1, en particular su interfaz adhesiva estructuralmente definida, codifica la especificidad funcional de las cadherinas de tipo II in vivo.
  • Las diferencias estructurales en las interfaces de dominio EC1 contribuyen a las distintas propiedades adhesivas de las cadherinas de tipo I y tipo II.