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Rab39a and Rab39b Display Different Intracellular Distribution and Function in Sphingolipids and Phospholipids Transport

Rab GTPases define the identity and destiny of vesicles. Some of these small GTPases present isoforms that are expressed differentially along developmental stages or in a tissue-specific manner, hence comparative analysis is difficult to achieve. Here, we describe the intracellular distribution and...

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Autores principales: Gambarte Tudela, Julián, Buonfigli, Julio, Luján, Agustín, Alonso Bivou, Mariano, Cebrián, Ignacio, Capmany, Anahí, Damiani, María Teresa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6480249/
https://www.ncbi.nlm.nih.gov/pubmed/30987349
http://dx.doi.org/10.3390/ijms20071688
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author Gambarte Tudela, Julián
Buonfigli, Julio
Luján, Agustín
Alonso Bivou, Mariano
Cebrián, Ignacio
Capmany, Anahí
Damiani, María Teresa
author_facet Gambarte Tudela, Julián
Buonfigli, Julio
Luján, Agustín
Alonso Bivou, Mariano
Cebrián, Ignacio
Capmany, Anahí
Damiani, María Teresa
author_sort Gambarte Tudela, Julián
collection PubMed
description Rab GTPases define the identity and destiny of vesicles. Some of these small GTPases present isoforms that are expressed differentially along developmental stages or in a tissue-specific manner, hence comparative analysis is difficult to achieve. Here, we describe the intracellular distribution and function in lipid transport of the poorly characterized Rab39 isoforms using typical cell biology experimental tools and new ones developed in our laboratory. We show that, despite their amino acid sequence similarity, Rab39a and Rab39b display non-overlapping intracellular distribution. Rab39a localizes in the late endocytic pathway, mainly at multivesicular bodies. In contrast, Rab39b distributes in the secretory network, at the endoplasmic reticulum/cis-Golgi interface. Therefore, Rab39a controls trafficking of lipids (sphingomyelin and phospholipids) segregated at multivesicular bodies, whereas Rab39b transports sphingolipids biosynthesized at the endoplasmic reticulum-Golgi factory. Interestingly, lyso bis-phosphatidic acid is exclusively transported by Rab39a, indicating that both isoforms do not exert identical functions in lipid transport. Conveniently, the requirement of eukaryotic lipids by the intracellular pathogen Chlamydia trachomatis rendered useful for dissecting and distinguishing Rab39a- and Rab39b-controlled trafficking pathways. Our findings provide comparative insights about the different subcellular distribution and function in lipid transport of the two Rab39 isoforms.
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spelling pubmed-64802492019-04-29 Rab39a and Rab39b Display Different Intracellular Distribution and Function in Sphingolipids and Phospholipids Transport Gambarte Tudela, Julián Buonfigli, Julio Luján, Agustín Alonso Bivou, Mariano Cebrián, Ignacio Capmany, Anahí Damiani, María Teresa Int J Mol Sci Article Rab GTPases define the identity and destiny of vesicles. Some of these small GTPases present isoforms that are expressed differentially along developmental stages or in a tissue-specific manner, hence comparative analysis is difficult to achieve. Here, we describe the intracellular distribution and function in lipid transport of the poorly characterized Rab39 isoforms using typical cell biology experimental tools and new ones developed in our laboratory. We show that, despite their amino acid sequence similarity, Rab39a and Rab39b display non-overlapping intracellular distribution. Rab39a localizes in the late endocytic pathway, mainly at multivesicular bodies. In contrast, Rab39b distributes in the secretory network, at the endoplasmic reticulum/cis-Golgi interface. Therefore, Rab39a controls trafficking of lipids (sphingomyelin and phospholipids) segregated at multivesicular bodies, whereas Rab39b transports sphingolipids biosynthesized at the endoplasmic reticulum-Golgi factory. Interestingly, lyso bis-phosphatidic acid is exclusively transported by Rab39a, indicating that both isoforms do not exert identical functions in lipid transport. Conveniently, the requirement of eukaryotic lipids by the intracellular pathogen Chlamydia trachomatis rendered useful for dissecting and distinguishing Rab39a- and Rab39b-controlled trafficking pathways. Our findings provide comparative insights about the different subcellular distribution and function in lipid transport of the two Rab39 isoforms. MDPI 2019-04-04 /pmc/articles/PMC6480249/ /pubmed/30987349 http://dx.doi.org/10.3390/ijms20071688 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Gambarte Tudela, Julián
Buonfigli, Julio
Luján, Agustín
Alonso Bivou, Mariano
Cebrián, Ignacio
Capmany, Anahí
Damiani, María Teresa
Rab39a and Rab39b Display Different Intracellular Distribution and Function in Sphingolipids and Phospholipids Transport
title Rab39a and Rab39b Display Different Intracellular Distribution and Function in Sphingolipids and Phospholipids Transport
title_full Rab39a and Rab39b Display Different Intracellular Distribution and Function in Sphingolipids and Phospholipids Transport
title_fullStr Rab39a and Rab39b Display Different Intracellular Distribution and Function in Sphingolipids and Phospholipids Transport
title_full_unstemmed Rab39a and Rab39b Display Different Intracellular Distribution and Function in Sphingolipids and Phospholipids Transport
title_short Rab39a and Rab39b Display Different Intracellular Distribution and Function in Sphingolipids and Phospholipids Transport
title_sort rab39a and rab39b display different intracellular distribution and function in sphingolipids and phospholipids transport
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6480249/
https://www.ncbi.nlm.nih.gov/pubmed/30987349
http://dx.doi.org/10.3390/ijms20071688
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