Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells
Autor(a) principal: | |
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Data de Publicação: | 1993 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRN |
Texto Completo: | https://repositorio.ufrn.br/handle/123456789/54380 https://doi.org/10.1242/jcs.1993.Supplement_17.6 |
Resumo: | The movement of newly synthesized proteins in the constitutive secretory pathway, from their site of synthesis in the endoplasmic reticulum to the cell surface or to intracellular destinations, requires an orderly sequence of transport steps between membrane-bound compartments. Until recently, the trafficking and secretion of proteins through this pathway was thought to occur as a relatively automatic, unregulated series of events. Recent studies show that protein trafficking in the constitutive secretory pathway requires G T P hydrolysis by families of GTP-binding proteins (G proteins), which at multiple steps potentially provide regulation and specificity for protein trafficking. M any monomeric G proteins are known to be localized and functional on membrane compartments in the constitutive secretory pathway. Now, members of the heterotrimeric G protein family have also been localized on intracellular membranes and compartments such as the Golgi complex. We have studied the localization and targeting of G a subunits to distinct membrane domains in polarized epithelial cells. The distribution of different G a subunits on very specific membrane domains in cultured epithelial cells and in epithelial cells of the kidney cortex, is highly suggestive of roles for these G proteins in intracellular trafficking pathways. One of these G protein subunits, Gai-3, was localized on Golgi membranes. Studies on L L C -P K i cells overexpressing Gcti.3 provided evidence for its functional role in regulating the transport o f a constitutively secreted heparan sulfate proteoglycan through the Golgi complex. Inhibition or activation of heterotrimeric G proteins by pertussis toxin or by aluminium fluoride respectively, have provided further evidence for regulation of intracellular transport by pertussis toxin-sensitive G proteins. Although the functions of Golgi-associated G proteins are not yet understood at the molecular level, heterotrimeric G proteins have been implicated in the binding of cytosolic coat proteins and vesicle formation on Golgi membranes. Future studies will elucidate how multiple G proteins, of both the heterotrimeric and monomeric families, are involved in the regulation of Golgi function and protein trafficking in the secretory pathway |
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Almeida, Jose Bruno deStow, Jennifer L.2023-08-03T19:45:53Z2023-08-03T19:45:53Z1993ALMEIDA, José Bruno de: STOW, Jennifer L. Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells. Journal Of Cell Science, [S.L.], v. 1993, n. 17, p. 33-39, 1 dez. 1993. The Company of Biologists. http://dx.doi.org/10.1242/jcs.1993.supplement_17.6. Disponível em: https://journals.biologists.com/jcs/article/1993/Supplement_17/33/58254/Distribution-and-role-of-heterotrimeric-G-proteins. Acesso em: 31 jul. 2023.https://repositorio.ufrn.br/handle/123456789/54380https://doi.org/10.1242/jcs.1993.Supplement_17.6Journal Of Cell Scienceg proteinsecretionvesicle traffickinggolgiDistribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cellsinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleThe movement of newly synthesized proteins in the constitutive secretory pathway, from their site of synthesis in the endoplasmic reticulum to the cell surface or to intracellular destinations, requires an orderly sequence of transport steps between membrane-bound compartments. Until recently, the trafficking and secretion of proteins through this pathway was thought to occur as a relatively automatic, unregulated series of events. Recent studies show that protein trafficking in the constitutive secretory pathway requires G T P hydrolysis by families of GTP-binding proteins (G proteins), which at multiple steps potentially provide regulation and specificity for protein trafficking. M any monomeric G proteins are known to be localized and functional on membrane compartments in the constitutive secretory pathway. Now, members of the heterotrimeric G protein family have also been localized on intracellular membranes and compartments such as the Golgi complex. We have studied the localization and targeting of G a subunits to distinct membrane domains in polarized epithelial cells. The distribution of different G a subunits on very specific membrane domains in cultured epithelial cells and in epithelial cells of the kidney cortex, is highly suggestive of roles for these G proteins in intracellular trafficking pathways. One of these G protein subunits, Gai-3, was localized on Golgi membranes. Studies on L L C -P K i cells overexpressing Gcti.3 provided evidence for its functional role in regulating the transport o f a constitutively secreted heparan sulfate proteoglycan through the Golgi complex. Inhibition or activation of heterotrimeric G proteins by pertussis toxin or by aluminium fluoride respectively, have provided further evidence for regulation of intracellular transport by pertussis toxin-sensitive G proteins. Although the functions of Golgi-associated G proteins are not yet understood at the molecular level, heterotrimeric G proteins have been implicated in the binding of cytosolic coat proteins and vesicle formation on Golgi membranes. Future studies will elucidate how multiple G proteins, of both the heterotrimeric and monomeric families, are involved in the regulation of Golgi function and protein trafficking in the secretory pathwayengreponame:Repositório Institucional da UFRNinstname:Universidade Federal do Rio Grande do Norte (UFRN)instacron:UFRNinfo:eu-repo/semantics/openAccessORIGINALDistributionRoleHeterotrimeric_Almeida_1993.pdfDistributionRoleHeterotrimeric_Almeida_1993.pdfapplication/pdf8693350https://repositorio.ufrn.br/bitstream/123456789/54380/1/DistributionRoleHeterotrimeric_Almeida_1993.pdf2d22abb7ac54c9577c33e5c5b5c05cd4MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81484https://repositorio.ufrn.br/bitstream/123456789/54380/2/license.txte9597aa2854d128fd968be5edc8a28d9MD52123456789/543802023-08-03 16:45:54.34oai:https://repositorio.ufrn.br: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Repositório de PublicaçõesPUBhttp://repositorio.ufrn.br/oai/opendoar:2023-08-03T19:45:54Repositório Institucional da UFRN - Universidade Federal do Rio Grande do Norte (UFRN)false |
dc.title.pt_BR.fl_str_mv |
Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells |
title |
Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells |
spellingShingle |
Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells Almeida, Jose Bruno de g protein secretion vesicle trafficking golgi |
title_short |
Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells |
title_full |
Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells |
title_fullStr |
Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells |
title_full_unstemmed |
Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells |
title_sort |
Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells |
author |
Almeida, Jose Bruno de |
author_facet |
Almeida, Jose Bruno de Stow, Jennifer L. |
author_role |
author |
author2 |
Stow, Jennifer L. |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Almeida, Jose Bruno de Stow, Jennifer L. |
dc.subject.por.fl_str_mv |
g protein secretion vesicle trafficking golgi |
topic |
g protein secretion vesicle trafficking golgi |
description |
The movement of newly synthesized proteins in the constitutive secretory pathway, from their site of synthesis in the endoplasmic reticulum to the cell surface or to intracellular destinations, requires an orderly sequence of transport steps between membrane-bound compartments. Until recently, the trafficking and secretion of proteins through this pathway was thought to occur as a relatively automatic, unregulated series of events. Recent studies show that protein trafficking in the constitutive secretory pathway requires G T P hydrolysis by families of GTP-binding proteins (G proteins), which at multiple steps potentially provide regulation and specificity for protein trafficking. M any monomeric G proteins are known to be localized and functional on membrane compartments in the constitutive secretory pathway. Now, members of the heterotrimeric G protein family have also been localized on intracellular membranes and compartments such as the Golgi complex. We have studied the localization and targeting of G a subunits to distinct membrane domains in polarized epithelial cells. The distribution of different G a subunits on very specific membrane domains in cultured epithelial cells and in epithelial cells of the kidney cortex, is highly suggestive of roles for these G proteins in intracellular trafficking pathways. One of these G protein subunits, Gai-3, was localized on Golgi membranes. Studies on L L C -P K i cells overexpressing Gcti.3 provided evidence for its functional role in regulating the transport o f a constitutively secreted heparan sulfate proteoglycan through the Golgi complex. Inhibition or activation of heterotrimeric G proteins by pertussis toxin or by aluminium fluoride respectively, have provided further evidence for regulation of intracellular transport by pertussis toxin-sensitive G proteins. Although the functions of Golgi-associated G proteins are not yet understood at the molecular level, heterotrimeric G proteins have been implicated in the binding of cytosolic coat proteins and vesicle formation on Golgi membranes. Future studies will elucidate how multiple G proteins, of both the heterotrimeric and monomeric families, are involved in the regulation of Golgi function and protein trafficking in the secretory pathway |
publishDate |
1993 |
dc.date.issued.fl_str_mv |
1993 |
dc.date.accessioned.fl_str_mv |
2023-08-03T19:45:53Z |
dc.date.available.fl_str_mv |
2023-08-03T19:45:53Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
ALMEIDA, José Bruno de: STOW, Jennifer L. Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells. Journal Of Cell Science, [S.L.], v. 1993, n. 17, p. 33-39, 1 dez. 1993. The Company of Biologists. http://dx.doi.org/10.1242/jcs.1993.supplement_17.6. Disponível em: https://journals.biologists.com/jcs/article/1993/Supplement_17/33/58254/Distribution-and-role-of-heterotrimeric-G-proteins. Acesso em: 31 jul. 2023. |
dc.identifier.uri.fl_str_mv |
https://repositorio.ufrn.br/handle/123456789/54380 |
dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1242/jcs.1993.Supplement_17.6 |
identifier_str_mv |
ALMEIDA, José Bruno de: STOW, Jennifer L. Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells. Journal Of Cell Science, [S.L.], v. 1993, n. 17, p. 33-39, 1 dez. 1993. The Company of Biologists. http://dx.doi.org/10.1242/jcs.1993.supplement_17.6. Disponível em: https://journals.biologists.com/jcs/article/1993/Supplement_17/33/58254/Distribution-and-role-of-heterotrimeric-G-proteins. Acesso em: 31 jul. 2023. |
url |
https://repositorio.ufrn.br/handle/123456789/54380 https://doi.org/10.1242/jcs.1993.Supplement_17.6 |
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eng |
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eng |
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Journal Of Cell Science |
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Journal Of Cell Science |
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