Mostrar el registro sencillo del ítem
dc.contributor.author
Grabski, Robert
dc.contributor.author
Balklava, Zita
dc.contributor.author
Wyrozumska, Paulina
dc.contributor.author
Szul, Tomasz
dc.contributor.author
Brandon, Elizabeth
dc.contributor.author
Alvarez, Cecilia Ines
dc.contributor.author
Holloway, Zoe G.
dc.contributor.author
Sztul, Elizabeth
dc.date.available
2018-08-13T17:39:22Z
dc.date.issued
2012-02
dc.identifier.citation
Grabski, Robert; Balklava, Zita; Wyrozumska, Paulina; Szul, Tomasz; Brandon, Elizabeth; et al.; Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking; Company of Biologists; Journal of Cell Science; 125; 8; 2-2012; 1896-1909
dc.identifier.issn
0021-9533
dc.identifier.uri
http://hdl.handle.net/11336/55149
dc.description.abstract
The tethering factor p115 (known as Uso1p in yeast) has been shown to facilitate Golgi biogenesis and membrane traffic in cells in culture. However, the role of p115 within an intact animal is largely unknown. Here, we document that depletion of p115 by using RNA interference (RNAi) in C. elegans causes accumulation of the 170 kD soluble yolk protein (YP170) in the body cavity and retention of the yolk receptor RME-2 in the ER and the Golgi within oocytes. Structure–function analyses of p115 have identified two homology regions (H1 and H2) within the N-terminal globular head and the coiled-coil 1 (CC1) domain as essential for p115 function. We identify a new C-terminal domain of p115 as necessary for Golgi ribbon formation and cargo trafficking. We show that p115 mutants that lack the fourth CC domain (CC4) act in a dominant-negative manner to disrupt Golgi and prevent cargo trafficking in cells containing endogenous p115. Furthermore, using RNAi of p115 and the subsequent transfection with p115 deletion mutants, we show that CC4 is necessary for Golgi ribbon formation and membrane trafficking in cells depleted of endogenous p115. p115 has been shown to bind a subset of ER-Golgi SNAREs through CC1 and CC4 domains (Shorter et al., 2002). Our findings show that CC4 is required for p115 function, and suggest that both the CC1 and the CC4 SNARE-binding motifs participate in p115-mediated membrane tethering.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Company of Biologists
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
P115
dc.subject
Trafficking
dc.subject
Golgi
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-08-08T18:15:31Z
dc.identifier.eissn
1477-9137
dc.journal.volume
125
dc.journal.number
8
dc.journal.pagination
1896-1909
dc.journal.pais
Reino Unido
dc.journal.ciudad
Cambridge
dc.description.fil
Fil: Grabski, Robert. University of Alabama at Birmingahm; Estados Unidos
dc.description.fil
Fil: Balklava, Zita. University of Alabama at Birmingahm; Estados Unidos
dc.description.fil
Fil: Wyrozumska, Paulina. University of Alabama at Birmingahm; Estados Unidos
dc.description.fil
Fil: Szul, Tomasz. University of Alabama at Birmingahm; Estados Unidos
dc.description.fil
Fil: Brandon, Elizabeth. University of Alabama at Birmingahm; Estados Unidos
dc.description.fil
Fil: Alvarez, Cecilia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
dc.description.fil
Fil: Holloway, Zoe G.. University of Alabama at Birmingahm; Estados Unidos
dc.description.fil
Fil: Sztul, Elizabeth. University of Alabama at Birmingahm; Estados Unidos
dc.journal.title
Journal of Cell Science
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4450726/
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1242%2Fjcs.090571
Archivos asociados