Monday, November 24, 2014

 

 



Soy un nuevo usuario

Olvidé mi contraseña

Entrada usuarios

Lógica Matemáticas Astronomía y Astrofísica Física Química Ciencias de la Vida
Ciencias de la Tierra y Espacio Ciencias Agrarias Ciencias Médicas Ciencias Tecnológicas Antropología Demografía
Ciencias Económicas Geografía Historia Ciencias Jurídicas y Derecho Lingüística Pedagogía
Ciencia Política Psicología Artes y Letras Sociología Ética Filosofía


Live-cell fluorescence correlation spectroscopy dissects the role of coregulator exchange and chromatin binding in retinoic acid receptor mobility

1) La descarga del recurso depende de la página de origen
2) Para poder descargar el recurso, es necesario ser usuario
    registrado en Universia


  Descargar recurso

Detalles del recurso

Pertenece a: PubMed Central (PMC3 - NLM DTD)  

Descripción: The retinoic acid receptor (RAR) is a member of the nuclear receptor superfamily. This ligand-inducible transcription factor binds to DNA as a heterodimer with the retinoid X receptor (RXR) in the nucleus. The nucleus is a dynamic compartment and live-cell imaging techniques make it possible to investigate transcription factor action in real-time. We studied the diffusion of EGFP–RAR by fluorescence correlation spectroscopy (FCS) to uncover the molecular interactions determining receptor mobility. In the absence of ligand, we identified two distinct species with different mobilities. The fast component has a diffusion coefficient of D1=1.8–6.0 μm2/second corresponding to small oligomeric forms, whereas the slow component with D2=0.05–0.10 μm2/second corresponds to interactions of RAR with the chromatin or other large structures. The RAR ligand-binding-domain fragment also has a slow component, probably as a result of indirect DNA-binding through RXR, with lower affinity than the intact RAR–RXR complex. Importantly, RAR-agonist treatment shifts the equilibrium towards the slow population of the wild-type receptor, but without significantly changing the mobility of either the fast or the slow population. By using a series of mutant forms of the receptor with altered DNA- or coregulator-binding capacity we found that the slow component is probably related to chromatin binding, and that coregulator exchange, specifically the binding of the coactivator complex, is the main determinant contributing to the redistribution of RAR during ligand activation.

Autor(es): Brazda, Peter -  Szekeres, Tibor -  Bravics, Balázs -  Tóth, Katalin -  Vámosi, György -  Nagy, Laszlo - 

Id.: 55236511

Idioma: English  - 

Versión: 1.0

Estado: Final

Palabras claveResearch Articles - 

Tipo de recurso: Text  - 

Tipo de Interactividad: Expositivo

Nivel de Interactividad: muy bajo

Audiencia: Estudiante  -  Profesor  -  Autor  - 

Estructura: Atomic

Coste: no

Copyright: sí

Requerimientos técnicos:  Browser: Any - 

Fecha de contribución: 02-may-2012

Contacto:

Localización:


Otros recursos del mismo autor(es)

  1. PPARγ activation but not PPARγ haplodeficiency affects proangiogenic potential of endothelial cells and bone marrow-derived progenitors
  2. A foglyokról, rabságról és a börtönökröl. "Dr. Klein S. német forditása után magyaritották Tóth Mór ... és Nagy László ..."
  3. Ligand Binding Shifts Highly Mobile Retinoid X Receptor to the Chromatin-Bound State in a Coactivator-Dependent Manner, as Revealed by Single-Cell Imaging Retinoid X receptor (RXR) is a promiscuous nuclear receptor forming heterodimers with several other ...
  4. Small but sturdy: small RNAs in cellular memory and epigenetics Cell identities can be stable over a long time due to a “cellular memory” of expression profiles ach...
  5. RDH10, RALDH2, and CRABP2 are required components of PPARγ-directed ATRA synthesis and signaling in human dendritic cells[S] All-trans retinoic acid (ATRA) has a key role in dendritic cells (DCs) and affects T cell subtype sp...

Otros recursos de la misma colección

  1. Cardiac ryanodine receptor activation by a high Ca2+ store load is reversed in a reducing cytoplasmic redox environment
  2. The PAR complex controls the spatiotemporal dynamics of F-actin and the MTOC in directionally migrating leukocytes
  3. The Arf family G protein Arl1 is required for secretory granule biogenesis in Drosophila The small G protein Arf like 1 (Arl1) is found at the Golgi complex, and its GTP-bound form recruits...
  4. Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors Dynamin, which is encoded by three genes in mammals, is a GTPase implicated in endocytic membrane fi...
  5. Centromeric motion facilitates the mobility of interphase genomic regions in fission yeast Dispersed genetic elements, such as retrotransposons and Pol-III-transcribed genes, including tRNA a...

Valoración de los usuarios

No hay ninguna valoración para este recurso.Sea el primero en valorar este recurso.
 

Busque un recurso