Sunday, January 25, 2015

 

 



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


Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome–nucleus association and transcriptional signaling

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 multifunctional structural protein 4.1R is required for assembly and maintenance of functional nuclei but its nuclear roles are unidentified. 4.1R localizes within nuclei, at the nuclear envelope, and in cytoplasm. Here we show that 4.1R, the nuclear envelope protein emerin and the intermediate filament protein lamin A/C co-immunoprecipitate, and that 4.1R-specific depletion in human cells by RNA interference produces nuclear dysmorphology and selective mislocalization of proteins from several nuclear subcompartments. Such 4.1R-deficiency causes emerin to partially redistribute into the cytoplasm, whereas lamin A/C is disorganized at nuclear rims and displaced from nucleoplasmic foci. The nuclear envelope protein MAN1, nuclear pore proteins Tpr and Nup62, and nucleoplasmic proteins NuMA and LAP2α also have aberrant distributions, but lamin B and LAP2β have normal localizations. 4.1R-deficient mouse embryonic fibroblasts show a similar phenotype. We determined the functional effects of 4.1R-deficiency that reflect disruption of the association of 4.1R with emerin and A-type lamin: increased nucleus–centrosome distances, increased β-catenin signaling, and relocalization of β-catenin from the plasma membrane to the nucleus. Furthermore, emerin- and lamin-A/C-null cells have decreased nuclear 4.1R. Our data provide evidence that 4.1R has important functional interactions with emerin and A-type lamin that impact upon nuclear architecture, centrosome–nuclear envelope association and the regulation of β-catenin transcriptional co-activator activity that is dependent on β-catenin nuclear export.

Autor(es): Meyer, Adam J. -  Almendrala, Donna K. -  Go, Minjoung M. -  Krauss, Sharon Wald - 

Id.: 55234385

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. Library Generation by Gene Shuffling
  2. Cloning of mDEAH9, a putative RNA helicase and mammalian homologue of Saccharomyces cerevisiae splicing factor Prp43 Yeast splicing factor Prp43, a DEAH box protein of the putative RNA helicase/RNA-dependent NTPase fa...
  3. A 'resource allocator' for transcription based on a highly fragmented T7 RNA polymerase Synthetic genetic systems share resources with the host, including machinery for transcription and t...
  4. Engagement of CD81 induces ezrin tyrosine phosphorylation and its cellular redistribution with filamentous actin CD81 is a tetraspanin family member involved in diverse cellular interactions in the immune and ner...
  5. Downregulation of Protein 4.1R, a Mature Centriole Protein, Disrupts Centrosomes, Alters Cell Cycle Progression, and Perturbs Mitotic Spindles and Anaphase? Centrosomes nucleate and organize interphase microtubules and are instrumental in mitotic bipolar sp...

Otros recursos de la misma colección

  1. Rab8a and Rab8b are essential for several apical transport pathways but insufficient for ciliogenesis The small GTP-binding protein Rab8 is known to play an essential role in intracellular transport and...
  2. Injury-triggered Akt phosphorylation of Cx43: a ZO-1-driven molecular switch that regulates gap junction size The proteins that form vertebrate gap junctions, the connexins, are highly regulated and have short ...
  3. Live-cell fluorescence imaging reveals high stoichiometry of Grb2 binding to the EGF receptor sustained during endocytosis Activation of epidermal growth factor (EGF) receptor (EGFR) leads to its interaction with Grb2, a du...
  4. The Smad7–Skp2 complex orchestrates Myc stability, impacting on the cytostatic effect of TGF-β In most human cancers the Myc proto-oncogene is highly activated. Dysregulation of Myc oncoprotein c...
  5. Phosphorylation of the E3 ubiquitin ligase RNF41 by the kinase Par-1b is required for epithelial cell polarity The establishment and maintenance of cell polarity is an essential property governing organismal hom...

Valoración de los usuarios

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

Busque un recurso