Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking
- Autores
- Grabski, Robert; Balklava, Zita; Wyrozumska, Paulina; Szul, Tomasz; Brandon, Elizabeth; Alvarez, Cecilia Ines; Holloway, Zoe G.; Sztul, Elizabeth
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
Fil: Grabski, Robert. University of Alabama at Birmingahm; Estados Unidos
Fil: Balklava, Zita. University of Alabama at Birmingahm; Estados Unidos
Fil: Wyrozumska, Paulina. University of Alabama at Birmingahm; Estados Unidos
Fil: Szul, Tomasz. University of Alabama at Birmingahm; Estados Unidos
Fil: Brandon, Elizabeth. University of Alabama at Birmingahm; Estados Unidos
Fil: Alvarez, Cecilia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Holloway, Zoe G.. University of Alabama at Birmingahm; Estados Unidos
Fil: Sztul, Elizabeth. University of Alabama at Birmingahm; Estados Unidos - Materia
-
p115
TRAFFICKING
GOLGI - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/55149
Ver los metadatos del registro completo
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network_name_str |
CONICET Digital (CONICET) |
spelling |
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane traffickingGrabski, RobertBalklava, ZitaWyrozumska, PaulinaSzul, TomaszBrandon, ElizabethAlvarez, Cecilia InesHolloway, Zoe G.Sztul, Elizabethp115TRAFFICKINGGOLGIhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The 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.Fil: Grabski, Robert. University of Alabama at Birmingahm; Estados UnidosFil: Balklava, Zita. University of Alabama at Birmingahm; Estados UnidosFil: Wyrozumska, Paulina. University of Alabama at Birmingahm; Estados UnidosFil: Szul, Tomasz. University of Alabama at Birmingahm; Estados UnidosFil: Brandon, Elizabeth. University of Alabama at Birmingahm; Estados UnidosFil: Alvarez, Cecilia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Holloway, Zoe G.. University of Alabama at Birmingahm; Estados UnidosFil: Sztul, Elizabeth. University of Alabama at Birmingahm; Estados UnidosCompany of Biologists2012-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/55149Grabski, 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; 1896-19090021-95331477-9137CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4450726/info:eu-repo/semantics/altIdentifier/doi/10.1242%2Fjcs.090571info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:49:25Zoai:ri.conicet.gov.ar:11336/55149instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:49:25.812CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking |
title |
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking |
spellingShingle |
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking Grabski, Robert p115 TRAFFICKING GOLGI |
title_short |
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking |
title_full |
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking |
title_fullStr |
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking |
title_full_unstemmed |
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking |
title_sort |
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking |
dc.creator.none.fl_str_mv |
Grabski, Robert Balklava, Zita Wyrozumska, Paulina Szul, Tomasz Brandon, Elizabeth Alvarez, Cecilia Ines Holloway, Zoe G. Sztul, Elizabeth |
author |
Grabski, Robert |
author_facet |
Grabski, Robert Balklava, Zita Wyrozumska, Paulina Szul, Tomasz Brandon, Elizabeth Alvarez, Cecilia Ines Holloway, Zoe G. Sztul, Elizabeth |
author_role |
author |
author2 |
Balklava, Zita Wyrozumska, Paulina Szul, Tomasz Brandon, Elizabeth Alvarez, Cecilia Ines Holloway, Zoe G. Sztul, Elizabeth |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
p115 TRAFFICKING GOLGI |
topic |
p115 TRAFFICKING GOLGI |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
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. Fil: Grabski, Robert. University of Alabama at Birmingahm; Estados Unidos Fil: Balklava, Zita. University of Alabama at Birmingahm; Estados Unidos Fil: Wyrozumska, Paulina. University of Alabama at Birmingahm; Estados Unidos Fil: Szul, Tomasz. University of Alabama at Birmingahm; Estados Unidos Fil: Brandon, Elizabeth. University of Alabama at Birmingahm; Estados Unidos Fil: Alvarez, Cecilia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina Fil: Holloway, Zoe G.. University of Alabama at Birmingahm; Estados Unidos Fil: Sztul, Elizabeth. University of Alabama at Birmingahm; Estados Unidos |
description |
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. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-02 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/55149 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 0021-9533 1477-9137 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/55149 |
identifier_str_mv |
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 0021-9533 1477-9137 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4450726/ info:eu-repo/semantics/altIdentifier/doi/10.1242%2Fjcs.090571 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Company of Biologists |
publisher.none.fl_str_mv |
Company of Biologists |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
_version_ |
1844613530281574400 |
score |
13.070432 |