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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/55149

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network_acronym_str CONICETDig
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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
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