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

Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

12.3K
Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
12.3K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.0K
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,...
7.0K
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

3.8K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
3.8K
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

10.9K
The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
10.9K
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

7.2K
G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical,...
7.2K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

19.4K
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
19.4K

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

A dormant TIL phenotype defines non-small cell lung carcinomas sensitive to immune checkpoint blockers.

Nature communications·2018
Same author

Whole-exome sequencing and immune profiling of early-stage lung adenocarcinoma with fully annotated clinical follow-up.

Annals of oncology : official journal of the European Society for Medical Oncology·2018
Same author

Mutation profiles in early-stage lung squamous cell carcinoma with clinical follow-up and correlation with markers of immune function.

Annals of oncology : official journal of the European Society for Medical Oncology·2017
Same author

Whole-exome sequencing and immune profiling of early-stage lung adenocarcinoma with fully annotated clinical follow-up.

Annals of oncology : official journal of the European Society for Medical Oncology·2016
Same author

[Differential diagnosis and treatment of neurogenic and psychogenic dysuria in case of overactive bladder syndrome].

Terapevticheskii arkhiv·2013
Same author

[Neurourological signs of chronic cerebral vascular diseases].

Zhurnal nevrologii i psikhiatrii imeni S.S. Korsakova·2013
Same journal

Whole-cell particle-based digital twin simulations from 4D lattice light-sheet microscopy data.

Cell·2026
Same journal

Systematic discovery of pathogen effector functions across human pathogens and pathways.

Cell·2026
Same journal

Structural basis for host membrane binding and remodeling by invading malaria parasites.

Cell·2026
Same journal

Multiscale integration of tissue and chromatin context converts cell heterogeneity into stable intestinal patterning.

Cell·2026
Same journal

Arc mediates intercellular tau transmission via extracellular vesicles.

Cell·2026
Same journal

Electromagnetic field-inducible in vivo gene switch for remote spatiotemporal control of gene expression.

Cell·2026
Ver todos los artículos relacionados

Video Experimental Relacionado

Updated: Mar 21, 2026

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

9.4K

Bases estructurales para la dimerización y activación de los receptores FGF.

A N Plotnikov1, J Schlessinger, S R Hubbard

  • 1Department of Pharmacology, New York University School of Medicine, New York 10016, USA.

Cell
|September 18, 1999
PubMed
Resumen
Este resumen es generado por máquina.

La estructura cristalina revela cómo el Factor de Crecimiento de Fibroblastos 2 (FGF2) se une al Receptor del Factor de Crecimiento de Fibroblastos 1 (FGFR1), formando un dímero. Esta estructura explica la dimerización del receptor inducida por el FGF y la heparina.

Más Videos Relacionados

Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis
10:43

Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis

Published on: November 6, 2019

7.4K
Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
09:16

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy

Published on: September 11, 2015

8.8K

Videos de Experimentos Relacionados

Last Updated: Mar 21, 2026

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
15:05

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

9.4K
Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis
10:43

Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis

Published on: November 6, 2019

7.4K
Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
09:16

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy

Published on: September 11, 2015

8.8K

Área de la Ciencia:

  • Biología Estructural Biología estructural.
  • La bioquímica es la bioquímica.
  • Biología Molecular Biología Molecular

Sus antecedentes:

  • El Factor de Crecimiento de Fibroblastos 2 (FGF2) es crucial para la señalización celular.
  • El receptor 1 del factor de crecimiento de los fibroblastos (FGFR1) media la señalización de FGF2.
  • Comprender las interacciones FGF2-FGFR1 es clave para descifrar las vías de crecimiento y diferenciación celular.

Objetivo del estudio:

  • Para determinar la estructura cristalina de FGF2 unido a los dominios 2 y 3 (D2 y D3) similares a las inmunoglobulinas de FGFR1.
  • Aclarar los mecanismos moleculares subyacentes a la formación y dimerización del complejo FGF2-FGFR1.
  • Proporcionar una base estructural para la dimerización del FGFR inducida por el FGF y la heparina.

Principales métodos:

  • Cristalografía de rayos X con una resolución de 2.8 A.
  • Análisis de la estructura compleja FGF2:FGFR1.
  • Identificación de las interfaces de interacción y los posibles sitios de unión de la heparina.

Principales resultados:

  • La estructura cristalina revela un doble dímero simétrico formado por dos complejos FGF2:FGFR1.
  • FGF2 interactúa extensamente con los dominios D2 y D3 de FGFR1 y el enlazador interdominio.
  • Un cañón cargado positivamente en FGFR1 se identifica como un sitio potencial de unión de heparina.
  • La estabilización de dimeros implica interacciones entre los dominios FGF2, D2 y los contactos D2-D2 entre los receptores.

Conclusiones:

  • La estructura cristalina proporciona un modelo molecular detallado del complejo FGF2-FGFR1.
  • Los hallazgos ofrecen información sobre el mecanismo de la dimerización del FGFR mediada por FGF y heparina.
  • Esta comprensión estructural unifica los datos bioquímicos existentes y apoya un modelo general para la activación del receptor.