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Article ; Online: Branched Actin Maintains Acetylated Microtubule Network in the Early Secretory Pathway.

Yoshimura, Azumi / Miserey-Lenkei, Stéphanie / Coudrier, Evelyne / Goud, Bruno

2021 Volume 11, Issue 1

Abstract: In the early secretory pathway, the delivery of anterograde cargoes from the endoplasmic reticulum (ER) exit sites (ERES) to the Golgi apparatus is a multi-step transport process occurring via the ER-Golgi intermediate compartment (IC, also called ERGIC). ...

Abstract	In the early secretory pathway, the delivery of anterograde cargoes from the endoplasmic reticulum (ER) exit sites (ERES) to the Golgi apparatus is a multi-step transport process occurring via the ER-Golgi intermediate compartment (IC, also called ERGIC). While the role microtubules in ER-to-Golgi transport has been well established, how the actin cytoskeleton contributes to this process remains poorly understood. Here, we report that Arp2/3 inhibition affects the network of acetylated microtubules around the Golgi and induces the accumulation of unusually long RAB1/GM130-positive carriers around the centrosome. These long carriers are less prone to reach the Golgi apparatus, and arrival of anterograde cargoes to the Golgi is decreased upon Arp2/3 inhibition. Our data suggest that Arp2/3-dependent actin polymerization maintains a stable network of acetylated microtubules, which ensures efficient cargo trafficking at the late stage of ER to Golgi transport.
MeSH term(s)	Acetylation ; Actin-Related Protein 2-3 Complex ; Actins/metabolism ; Autoantigens/metabolism ; Centrosome/metabolism ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Green Fluorescent Proteins/metabolism ; HeLa Cells ; Humans ; Membrane Proteins/metabolism ; Microtubules/metabolism ; Secretory Pathway ; rab1 GTP-Binding Proteins/metabolism
Chemical Substances	Actin-Related Protein 2-3 Complex ; Actins ; Autoantigens ; Golgin subfamily A member 2 ; Membrane Proteins ; Green Fluorescent Proteins (147336-22-9) ; rab1 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2021-12-22
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11010015
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Article ; Online: Branched Actin Maintains Acetylated Microtubule Network in the Early Secretory Pathway

Azumi Yoshimura / Stéphanie Miserey-Lenkei / Evelyne Coudrier / Bruno Goud

Cells, Vol 11, Iss 15, p

2022 Volume 15

Abstract	In the early secretory pathway, the delivery of anterograde cargoes from the endoplasmic reticulum (ER) exit sites (ERES) to the Golgi apparatus is a multi-step transport process occurring via the ER-Golgi intermediate compartment (IC, also called ERGIC). While the role microtubules in ER-to-Golgi transport has been well established, how the actin cytoskeleton contributes to this process remains poorly understood. Here, we report that Arp2/3 inhibition affects the network of acetylated microtubules around the Golgi and induces the accumulation of unusually long RAB1/GM130-positive carriers around the centrosome. These long carriers are less prone to reach the Golgi apparatus, and arrival of anterograde cargoes to the Golgi is decreased upon Arp2/3 inhibition. Our data suggest that Arp2/3-dependent actin polymerization maintains a stable network of acetylated microtubules, which ensures efficient cargo trafficking at the late stage of ER to Golgi transport.
Keywords	membrane trafficking ; Golgi apparatus ; RAB1 GTPase ; Arp2/3 ; microtubules ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2022-12-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: RAB6 GTPase regulates mammary secretory function by controlling the activation of STAT5.

Cayre, Surya / Faraldo, Marisa M / Bardin, Sabine / Miserey-Lenkei, Stéphanie / Deugnier, Marie-Ange / Goud, Bruno

Development (Cambridge, England)

2020 Volume 147, Issue 19

Abstract: The Golgi-associated RAB GTPases, RAB6A and RAB6A', regulate anterograde and retrograde transport pathways from and to the Golgi. ...

Abstract	The Golgi-associated RAB GTPases, RAB6A and RAB6A', regulate anterograde and retrograde transport pathways from and to the Golgi.
MeSH term(s)	Animals ; Blotting, Western ; Cell Line ; Female ; Flow Cytometry ; Humans ; In Situ Nick-End Labeling ; Mammary Glands, Human/cytology ; Mammary Glands, Human/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mice, Transgenic ; STAT5 Transcription Factor/genetics ; STAT5 Transcription Factor/metabolism ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
Chemical Substances	STAT5 Transcription Factor ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2020-10-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	90607-4
ISSN	1477-9129 ; 0950-1991
ISSN (online)	1477-9129
ISSN	0950-1991
DOI	10.1242/dev.190744
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Article: Small RAB GTPases Regulate Multiple Steps of Mitosis.

Miserey-Lenkei, Stéphanie / Colombo, María I

Frontiers in cell and developmental biology

2016 Volume 4, Page(s) 2

Abstract: GTPases of the RAB family are key regulators of multiple steps of membrane trafficking. Several members of the RAB GTPase family have been implicated in mitotic progression. In this review, we will first focus on the function of endosome-associated RAB ... ...

Abstract	GTPases of the RAB family are key regulators of multiple steps of membrane trafficking. Several members of the RAB GTPase family have been implicated in mitotic progression. In this review, we will first focus on the function of endosome-associated RAB GTPases reported in early steps of mitosis, spindle pole maturation, and during cytokinesis. Second, we will discuss the role of Golgi-associated RAB GTPases at the metaphase/anaphase transition and during cytokinesis.
Language	English
Publishing date	2016-02-17
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2016.00002
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Article ; Online: Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.

Ranaivoson, Fanomezana Moutse / Crozet, Vincent / Benoit, Matthieu P M H / Abdalla Mohammed Khalid, Amna / Kikuti, Carlos / Sirkia, Helena / El Marjou, Ahmed / Miserey-Lenkei, Stéphanie / Asenjo, Ana B / Sosa, Hernando / Schmidt, Christoph F / Rosenfeld, Steven S / Houdusse, Anne

Open biology

2023 Volume 13, Issue 9, Page(s) 230122

Abstract: KIF20A is a critical kinesin for cell division and a promising anti-cancer drug target. The mechanisms underlying its cellular roles remain elusive. Interestingly, unusual coupling between the nucleotide- and microtubule-binding sites of this kinesin-6 ... ...

Abstract	KIF20A is a critical kinesin for cell division and a promising anti-cancer drug target. The mechanisms underlying its cellular roles remain elusive. Interestingly, unusual coupling between the nucleotide- and microtubule-binding sites of this kinesin-6 has been reported, but little is known about how its divergent sequence leads to atypical motility properties. We present here the first high-resolution structure of its motor domain that delineates the highly unusual structural features of this motor, including a long L6 insertion that integrates into the core of the motor domain and that drastically affects allostery and ATPase activity. Together with the high-resolution cryo-electron microscopy microtubule-bound KIF20A structure that reveals the microtubule-binding interface, we dissect the peculiarities of the KIF20A sequence that influence its mechanochemistry, leading to low motility compared to other kinesins. Structural and functional insights from the KIF20A pre-power stroke conformation highlight the role of extended insertions in shaping the motor's mechanochemical cycle. Essential for force production and processivity is the length of the neck linker in kinesins. We highlight here the role of the sequence preceding the neck linker in controlling its backward docking and show that a neck linker four times longer than that in kinesin-1 is required for the activity of this motor.
MeSH term(s)	Cryoelectron Microscopy ; Kinesins/genetics ; Binding Sites ; Cell Division ; Microtubules
Chemical Substances	Kinesins (EC 3.6.4.4)
Language	English
Publishing date	2023-09-20
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2630944-0
ISSN	2046-2441 ; 2046-2441
ISSN (online)	2046-2441
ISSN	2046-2441
DOI	10.1098/rsob.230122
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Article ; Online: Analysis of the interactions between Rab GTPases and class V myosins.

Lindsay, Andrew J / Miserey-Lenkei, Stéphanie / Goud, Bruno

Methods in molecular biology (Clifton, N.J.)

2015 Volume 1298, Page(s) 73–83

Abstract: Myosins are actin-based motor proteins that are involved in a wide variety of cellular processes such as membrane transport, muscle contraction, and cell division. Humans have over 40 myosins that can be placed into 18 classes, the malfunctioning of a ... ...

Abstract	Myosins are actin-based motor proteins that are involved in a wide variety of cellular processes such as membrane transport, muscle contraction, and cell division. Humans have over 40 myosins that can be placed into 18 classes, the malfunctioning of a number of which can lead to disease. There are three members of the human class V myosin family, myosins Va, Vb, and Vc. People lacking functional myosin Va suffer from a rare autosomal recessive disease called Griscelli's Syndrome type I (GS1) that is characterized by severe neurological defects and partial albinism. Mutations in the myosin Vb gene lead to an epithelial disorder called microvillus inclusion disease (MVID) that is often fatal in infants. The class V myosins have been implicated in the transport of diverse cargoes such as melanosomes in pigment cells, synaptic vesicles in neurons, RNA transcripts in a variety of cell types, and organelles such as the endoplasmic reticulum. The Rab GTPases play a critical role in recruiting class V myosins to their cargo. We recently published a study in which we used the yeast two-hybrid system to systematically test myosin Va for its ability to interact with each member of the human Rab GTPase family. We present here a detailed description of this yeast two-hybrid "living chip" assay. Furthermore, we present a protocol for validating positive interactions obtained from this screen by coimmunoprecipitation.
MeSH term(s)	Humans ; Immunoprecipitation ; Myosin Type V/isolation & purification ; Myosin Type V/metabolism ; Protein Binding ; Two-Hybrid System Techniques/instrumentation ; rab GTP-Binding Proteins/isolation & purification ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Myosin Type V (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-2569-8_6
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Article ; Online: A comprehensive library of fluorescent constructs of SARS-CoV-2 proteins and their initial characterisation in different cell types.

Miserey-Lenkei, Stéphanie / Trajkovic, Katarina / D'Ambrosio, Juan Martín / Patel, Amanda J / Čopič, Alenka / Mathur, Pallavi / Schauer, Kristine / Goud, Bruno / Albanèse, Véronique / Gautier, Romain / Subra, Melody / Kovacs, David / Barelli, Hélène / Antonny, Bruno

Biology of the cell

2021 Volume 113, Issue 7, Page(s) 311–328

Abstract: Background information: Comprehensive libraries of plasmids for SARS-CoV-2 proteins with various tags (e.g., Strep, HA, Turbo) are now available. They enable the identification of numerous potential protein-protein interactions between the SARS-CoV-2 ... ...

Abstract	Background information: Comprehensive libraries of plasmids for SARS-CoV-2 proteins with various tags (e.g., Strep, HA, Turbo) are now available. They enable the identification of numerous potential protein-protein interactions between the SARS-CoV-2 virus and host proteins. Results: We present here a large library of SARS CoV-2 protein constructs fused with green and red fluorescent proteins and their initial characterisation in various human cell lines including lung epithelial cell models (A549, BEAS-2B), as well as in budding yeast. The localisation of a few SARS-CoV-2 proteins matches their proposed interactions with host proteins. These include the localisation of Nsp13 to the centrosome, Orf3a to late endosomes and Orf9b to mitochondria. Conclusions and significance: This library should facilitate further cellular investigations, notably by imaging techniques.
MeSH term(s)	A549 Cells ; COVID-19/virology ; Cell Line ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Host Microbial Interactions/physiology ; Humans ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Microscopy, Fluorescence ; Peptide Library ; Protein Interaction Domains and Motifs ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Time-Lapse Imaging ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Red Fluorescent Protein
Chemical Substances	Luminescent Proteins ; Peptide Library ; Recombinant Fusion Proteins ; Viral Proteins ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2021-05-10
Publishing country	England
Document type	Journal Article
ZDB-ID	245745-3
ISSN	1768-322X ; 0399-0311 ; 0248-4900
ISSN (online)	1768-322X
ISSN	0399-0311 ; 0248-4900
DOI	10.1111/boc.202000158
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Article ; Online: RAB6 and dynein drive post-Golgi apical transport to prevent neuronal progenitor delamination.

Brault, Jean-Baptiste / Bardin, Sabine / Lampic, Marusa / Carpentieri, Jacopo A / Coquand, Laure / Penisson, Maxime / Lachuer, Hugo / Victoria, Guiliana Soraya / Baloul, Sarah / El Marjou, Fatima / Boncompain, Gaelle / Miserey-Lenkei, Stephanie / Belvindrah, Richard / Fraisier, Vincent / Francis, Fiona / Perez, Franck / Goud, Bruno / Baffet, Alexandre D

EMBO reports

2022 Volume 23, Issue 10, Page(s) e54605

Abstract: Radial glial (RG) cells are the neural stem cells of the developing neocortex. Apical RG (aRG) cells can delaminate to generate basal RG (bRG) cells, a cell type associated with human brain expansion. Here, we report that aRG delamination is regulated by ...

Abstract	Radial glial (RG) cells are the neural stem cells of the developing neocortex. Apical RG (aRG) cells can delaminate to generate basal RG (bRG) cells, a cell type associated with human brain expansion. Here, we report that aRG delamination is regulated by the post-Golgi secretory pathway. Using in situ subcellular live imaging, we show that post-Golgi transport of RAB6+ vesicles occurs toward the minus ends of microtubules and depends on dynein. We demonstrate that the apical determinant Crumbs3 (CRB3) is also transported by dynein. Double knockout of RAB6A/A' and RAB6B impairs apical localization of CRB3 and induces a retraction of aRG cell apical process, leading to delamination and ectopic division. These defects are phenocopied by knockout of the dynein activator LIS1. Overall, our results identify a RAB6-dynein-LIS1 complex for Golgi to apical surface transport in aRG cells, and highlights the role of this pathway in the maintenance of neuroepithelial integrity.
MeSH term(s)	Dyneins/genetics ; Dyneins/metabolism ; Golgi Apparatus/metabolism ; Humans ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/metabolism ; Neurons/metabolism ; rab GTP-Binding Proteins/genetics ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Microtubule-Associated Proteins ; Dyneins (EC 3.6.4.2) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-08-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.202254605
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Article ; Online: Non-conventional Axonal Organelles Control TRPM8 Ion Channel Trafficking and Peripheral Cold Sensing.

Cornejo, Víctor Hugo / González, Carolina / Campos, Matías / Vargas-Saturno, Leslie / Juricic, María de Los Ángeles / Miserey-Lenkei, Stéphanie / Pertusa, María / Madrid, Rodolfo / Couve, Andrés

Cell reports

2020 Volume 30, Issue 13, Page(s) 4505–4517.e5

Abstract: TRPM8 is the main ion channel responsible for cold transduction in the somatosensory system. Nerve terminal availability of TRPM8 determines cold sensitivity, but how axonal secretory organelles control channel delivery remains poorly understood. Here we ...

Abstract	TRPM8 is the main ion channel responsible for cold transduction in the somatosensory system. Nerve terminal availability of TRPM8 determines cold sensitivity, but how axonal secretory organelles control channel delivery remains poorly understood. Here we examine the distribution of TRPM8 and trafficking organelles in cold-sensitive peripheral axons and disrupt trafficking by targeting the ARF-GEF GBF1 pharmacologically or the small GTPase RAB6 by optogenetics. In axons of the sciatic nerve, inhibition of GBF1 interrupts TRPM8 trafficking and increases association with the trans-Golgi network, LAMP1, and Golgi satellites, which distribute profusely along the axonal shaft. Accordingly, both TRPM8-dependent ongoing activity and cold-evoked responses reversibly decline upon GBF1 inhibition in nerve endings of corneal cold thermoreceptors. Inhibition of RAB6, which also associates to Golgi satellites, decreases cold-induced responses in vivo. Our results support a non-conventional axonal trafficking mechanism controlling the availability of TRPM8 in axons and cold sensitivity in the peripheral nervous system.
MeSH term(s)	Animals ; Axons/drug effects ; Axons/metabolism ; Cold Temperature ; Golgi Apparatus/drug effects ; Golgi Apparatus/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; HEK293 Cells ; HeLa Cells ; Humans ; Male ; Menthol/pharmacology ; Mice ; Optogenetics ; Organelles/drug effects ; Organelles/metabolism ; Protein Binding/drug effects ; Protein Transport/drug effects ; Sciatic Nerve/drug effects ; Sciatic Nerve/metabolism ; TRPM Cation Channels/metabolism ; Thermoreceptors/metabolism ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Gbf1 protein, mouse ; Guanine Nucleotide Exchange Factors ; Rab6 protein ; TRPM Cation Channels ; TRPM8 protein, mouse ; Menthol (1490-04-6) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2020-04-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2020.03.017
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Article ; Online: Phenotypic characterisation of RAB6A knockout mouse embryonic fibroblasts.

Bardin, Sabine / Miserey-Lenkei, Stéphanie / Hurbain, Ilse / Garcia-Castillo, Daniela / Raposo, Graça / Goud, Bruno

Biology of the cell

2015 Volume 107, Issue 12, Page(s) 427–439

Abstract: Background information: Rab6 is one of the most conserved Rab GTPaes throughout evolution and the most abundant Rab protein associated with the Golgi complex. The two ubiquitous Rab isoforms, Rab6A and Rab6A', that are generated by alternative splicing ... ...

Abstract	Background information: Rab6 is one of the most conserved Rab GTPaes throughout evolution and the most abundant Rab protein associated with the Golgi complex. The two ubiquitous Rab isoforms, Rab6A and Rab6A', that are generated by alternative splicing of the RAB6A gene, regulate several transport steps at the Golgi level, including retrograde transport between endosomes and Golgi, anterograde transport between Golgi and the plasma membrane, and intra-Golgi and Golgi to endoplasmic reticulum transport. Results: We have generated mice with a conditional null allele of RAB6A. Mice homozygous for the RAB6A null allele died at an early stage of embryonic development. Mouse embryonic fibroblasts (MEFs) were isolated from RAB6A(loxP/loxP) Rosa26-CreERT2 and incubated with 4-hydroxy tamoxifen, resulting in the efficient depletion of Rab6A and Rab6A'. We show that Rab6 depletion affects cell growth, alters Golgi morphology and decreases the Golgi-associated levels of some known Rab6 effectors such as Bicaudal-D and myosin II. We also show that Rab6 depletion protects MEFs against ricin toxin and delays VSV-G secretion. Conclusions: Our study shows that RAB6 is an essential gene required for normal embryonic development. We confirm in MEF cells most of the functions previously attributed to the two ubiquitous Rab6 isoforms.
MeSH term(s)	Alternative Splicing/genetics ; Animals ; Cell Membrane/drug effects ; Cell Membrane/genetics ; Embryonic Development/genetics ; Endoplasmic Reticulum/drug effects ; Endoplasmic Reticulum/metabolism ; Fibroblasts/drug effects ; Gene Expression Regulation, Developmental/drug effects ; Golgi Apparatus/drug effects ; Golgi Apparatus/metabolism ; Humans ; Mice ; Mice, Knockout ; Ricin/toxicity ; Tamoxifen/administration & dosage ; rab GTP-Binding Proteins/biosynthesis ; rab GTP-Binding Proteins/genetics
Chemical Substances	Rab6 protein ; Tamoxifen (094ZI81Y45) ; Ricin (9009-86-3) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2015-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	245745-3
ISSN	1768-322X ; 0399-0311 ; 0248-4900
ISSN (online)	1768-322X
ISSN	0399-0311 ; 0248-4900
DOI	10.1111/boc.201400083
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