Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells

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...

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Principais autores: Almeida, Jose Bruno de, Stow, Jennifer L.
Formato: article
Idioma:English
Publicado em: Journal Of Cell Science
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Endereço do item:https://repositorio.ufrn.br/handle/123456789/54380
https://doi.org/10.1242/jcs.1993.Supplement_17.6
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spelling ri-123456789-543802023-08-03T19:45:54Z Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells Almeida, Jose Bruno de Stow, Jennifer L. g protein secretion vesicle trafficking golgi 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 2023-08-03T19:45:53Z 2023-08-03T19:45:53Z 1993 article 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. https://repositorio.ufrn.br/handle/123456789/54380 https://doi.org/10.1242/jcs.1993.Supplement_17.6 en application/pdf Journal Of Cell Science
institution Repositório Institucional
collection RI - UFRN
language English
topic g protein
secretion
vesicle trafficking
golgi
spellingShingle g protein
secretion
vesicle trafficking
golgi
Almeida, Jose Bruno de
Stow, Jennifer L.
Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells
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
format article
author Almeida, Jose Bruno de
Stow, Jennifer L.
author_facet Almeida, Jose Bruno de
Stow, Jennifer L.
author_sort Almeida, Jose Bruno de
title Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells
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
publisher Journal Of Cell Science
publishDate 2023
url https://repositorio.ufrn.br/handle/123456789/54380
https://doi.org/10.1242/jcs.1993.Supplement_17.6
work_keys_str_mv AT almeidajosebrunode distributionandroleofheterotrimericgproteinsinthesecretorypathwayofpolarizedepithelialcells
AT stowjenniferl distributionandroleofheterotrimericgproteinsinthesecretorypathwayofpolarizedepithelialcells
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