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Article ; Online: Another hijack! Some enteroviruses co-opt the c10orf76/PI4KB complex for their own good.

Voilquin, Laetitia / Di Mattia, Thomas / Alpy, Fabien

2020 Volume 21, Issue 2, Page(s) e49876

Abstract: Enteroviruses, members of the Picornaviridae family, are non-enveloped and single-stranded RNA viruses responsible for several human diseases. During infection, these viruses build membrane-bound organelles, called replication organelles (ROs), where new ...

Abstract	Enteroviruses, members of the Picornaviridae family, are non-enveloped and single-stranded RNA viruses responsible for several human diseases. During infection, these viruses build membrane-bound organelles, called replication organelles (ROs), where new virions are assembled. ROs are highly enriched in phosphatidylinositol 4-phosphate (PI4P) produced by the host lipid kinase PI4KB. In this issue of EMBO Reports, McPhail et al [1] characterize a complex, formed by PI4KB and the c10orf76 protein, which is involved in PI4P production. They show that this machinery is hijacked by specific enteroviruses such as coxsackievirus A10 for their replication.
MeSH term(s)	Enterovirus ; Golgi Apparatus ; Humans ; Organelles ; Phosphotransferases (Alcohol Group Acceptor) ; Virus Replication
Chemical Substances	Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-)
Language	English
Publishing date	2020-01-09
Publishing country	England
Document type	News ; Comment
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.201949876
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Article ; Online: Faraway, so close! Functions of Endoplasmic reticulum-Endosome contacts.

Di Mattia, Thomas / Tomasetto, Catherine / Alpy, Fabien

Biochimica et biophysica acta. Molecular and cell biology of lipids

2019 Volume 1865, Issue 1, Page(s) 158490

Abstract: Eukaryotic cells are partitioned into functionally distinct organelles. Long considered as independent units in the cytosol, organelles are actually in constant and direct interaction with each other, mostly through the establishment of physical ... ...

Abstract	Eukaryotic cells are partitioned into functionally distinct organelles. Long considered as independent units in the cytosol, organelles are actually in constant and direct interaction with each other, mostly through the establishment of physical connections named membrane contact sites. Membrane contact sites constitute specific active regions involved in organelle dynamics, inter-organelle exchanges and communications. The endoplasmic reticulum (ER), which spreads throughout the cytosol, forms an extensive network that has many connections with the other organelles of the cell. Ample connections between the ER and endocytic organelles are observed in many cell types, highlighting their prominent physiological roles. Even though morphologically similar - a contact is a contact -, the identity of ER-Endosome contacts is defined by their specific molecular composition, which in turn determines the function of the contact. Here, we review the molecular mechanisms of ER-Endosome contact site formation and their associated cellular functions. This article is part of a Special Issue entitled Endoplasmic reticulum platforms for lipid dynamics edited by Shamshad Cockcroft and Christopher Stefan.
MeSH term(s)	Animals ; Biological Transport ; Calcium Signaling ; Cell Membrane/metabolism ; Endoplasmic Reticulum/metabolism ; Endosomes/metabolism ; Humans ; Lipid Metabolism
Language	English
Publishing date	2019-06-26
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2618 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2618 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbalip.2019.06.016
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Article ; Online: MOSPD2, un connecteur inter-organites.

Di Mattia, Thomas / Tomasetto, Catherine / Alpy, Fabien

Medecine sciences : M/S

2019 Volume 35, Issue 1, Page(s) 23–25

Title translation	MOSPD2, an inter-organelle connector.
MeSH term(s)	Animals ; Cytoplasm/metabolism ; Extracellular Fluid/metabolism ; Humans ; Intracellular Membranes/metabolism ; Membrane Proteins/physiology ; Organelles/metabolism ; Receptors, Chemokine/physiology
Chemical Substances	MOSPD2 protein, human ; Membrane Proteins ; Receptors, Chemokine
Language	French
Publishing date	2019-01-23
Publishing country	France
Document type	News
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2018313
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Article ; Online: A genetic screen to uncover mechanisms underlying lipid transfer protein function at membrane contact sites.

Mishra, Shirish / Manohar, Vaishnavi / Chandel, Shabnam / Manoj, Tejaswini / Bhattacharya, Subhodeep / Hegde, Nidhi / Nath, Vaisaly R / Krishnan, Harini / Wendling, Corinne / Di Mattia, Thomas / Martinet, Arthur / Chimata, Prasanth / Alpy, Fabien / Raghu, Padinjat

Life science alliance

2024 Volume 7, Issue 6

Abstract: Lipid transfer proteins mediate the transfer of lipids between organelle membranes, and the loss of function of these proteins has been linked to neurodegeneration. However, the mechanism by which loss of lipid transfer activity leads to ... ...

Abstract	Lipid transfer proteins mediate the transfer of lipids between organelle membranes, and the loss of function of these proteins has been linked to neurodegeneration. However, the mechanism by which loss of lipid transfer activity leads to neurodegeneration is not understood. In
MeSH term(s)	Animals ; Humans ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Retinal Degeneration/genetics ; Drosophila/genetics ; Drosophila/metabolism ; Phospholipid Transfer Proteins/genetics ; Lipids ; Carrier Proteins
Chemical Substances	lipid transfer protein ; Drosophila Proteins ; Phospholipid Transfer Proteins ; Lipids ; Carrier Proteins
Language	English
Publishing date	2024-03-18
Publishing country	United States
Document type	Journal Article
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.202302525
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Article: Faraway, so close! Functions of Endoplasmic reticulum–Endosome contacts

Di Mattia, Thomas / Alpy, Fabien / Tomasetto, Catherine

Biochimica et biophysica acta. 2019 June 20,

2019

Abstract	Eukaryotic cells are partitioned into functionally distinct organelles. Long considered as independent units in the cytosol, organelles are actually in constant and direct interaction with each other, mostly through the establishment of physical connections named membrane contact sites. Membrane contact sites constitute specific active regions involved in organelle dynamics, inter-organelle exchanges and communications. The endoplasmic reticulum (ER), which spreads throughout the cytosol, forms an extensive network that has many connections with the other organelles of the cell. Ample connections between the ER and endocytic organelles are observed in many cell types, highlighting their prominent physiological roles. Even though morphologically similar – a contact is a contact –, the identity of ER-Endosome contacts is defined by their specific molecular composition, which in turn determines the function of the contact. Here, we review the molecular mechanisms of ER-Endosome contact site formation and their associated cellular functions.This article is part of a Special Issue entitled Endoplasmic reticulum platforms for lipid dynamics edited by Shamshad Cockcroft and Christopher Stefan.
Keywords	cytosol ; endoplasmic reticulum ; eukaryotic cells ; lipids
Language	English
Dates of publication	2019-0620
Publishing place	Elsevier B.V.
Document type	Article
Note	Pre-press version
ISSN	1388-1981
DOI	10.1016/j.bbalip.2019.06.016
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Article ; Online: Cingulin and paracingulin tether myosins-2 to junctions to mechanoregulate the plasma membrane.

Rouaud, Florian / Huang, Wenmao / Flinois, Arielle / Jain, Kunalika / Vasileva, Ekaterina / Di Mattia, Thomas / Mauperin, Marine / Parry, David A D / Dugina, Vera / Chaponnier, Christine / Méan, Isabelle / Montessuit, Sylvie / Mutero-Maeda, Annick / Yan, Jie / Citi, Sandra

The Journal of cell biology

2023 Volume 222, Issue 7

Abstract: The mechanisms that regulate the spatial sorting of nonmuscle myosins-2 (NM2) isoforms and couple them mechanically to the plasma membrane are unclear. Here we show that the cytoplasmic junctional proteins cingulin (CGN) and paracingulin (CGNL1) interact ...

Abstract	The mechanisms that regulate the spatial sorting of nonmuscle myosins-2 (NM2) isoforms and couple them mechanically to the plasma membrane are unclear. Here we show that the cytoplasmic junctional proteins cingulin (CGN) and paracingulin (CGNL1) interact directly with NM2s through their C-terminal coiled-coil sequences. CGN binds strongly to NM2B, and CGNL1 to NM2A and NM2B. Knockout (KO), exogenous expression, and rescue experiments with WT and mutant proteins show that the NM2-binding region of CGN is required for the junctional accumulation of NM2B, ZO-1, ZO-3, and phalloidin-labeled actin filaments, and for the maintenance of tight junction membrane tortuosity and apical membrane stiffness. CGNL1 expression promotes the junctional accumulation of both NM2A and NM2B and its KO results in myosin-dependent fragmentation of adherens junction complexes. These results reveal a mechanism for the junctional localization of NM2A and NM2B and indicate that, by binding to NM2s, CGN and CGNL1 mechanically couple the actomyosin cytoskeleton to junctional protein complexes to mechanoregulate the plasma membrane.
MeSH term(s)	Adherens Junctions/metabolism ; Cell Membrane/metabolism ; Cytoskeletal Proteins/metabolism ; Cytoskeleton/metabolism ; Myosins/metabolism ; Tight Junctions/metabolism
Chemical Substances	Cytoskeletal Proteins ; Myosins (EC 3.6.4.1)
Language	English
Publishing date	2023-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202208065
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Article ; Online: MOSPD2 is an endoplasmic reticulum-lipid droplet tether functioning in LD homeostasis.

The Journal of cell biology

2022 Volume 221, Issue 6

Abstract: Membrane contact sites between organelles are organized by protein bridges. Among the components of these contacts, the VAP family comprises ER-anchored proteins, such as MOSPD2, that function as major ER-organelle tethers. MOSPD2 distinguishes itself ... ...

Abstract	Membrane contact sites between organelles are organized by protein bridges. Among the components of these contacts, the VAP family comprises ER-anchored proteins, such as MOSPD2, that function as major ER-organelle tethers. MOSPD2 distinguishes itself from the other members of the VAP family by the presence of a CRAL-TRIO domain. In this study, we show that MOSPD2 forms ER-lipid droplet (LD) contacts, thanks to its CRAL-TRIO domain. MOSPD2 ensures the attachment of the ER to LDs through a direct protein-membrane interaction. The attachment mechanism involves an amphipathic helix that has an affinity for lipid packing defects present at the surface of LDs. Remarkably, the absence of MOSPD2 markedly disturbs the assembly of lipid droplets. These data show that MOSPD2, in addition to being a general ER receptor for inter-organelle contacts, possesses an additional tethering activity and is specifically implicated in the biology of LDs via its CRAL-TRIO domain.
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Homeostasis ; Lipid Droplets/metabolism ; Membrane Proteins/metabolism ; Mitochondrial Membranes ; Receptors, Chemokine/metabolism
Chemical Substances	Membrane Proteins ; Receptors, Chemokine
Language	English
Publishing date	2022-04-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202110044
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Article ; Online: FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts.

Di Mattia, Thomas / Martinet, Arthur / Ikhlef, Souade / McEwen, Alastair G / Nominé, Yves / Wendling, Corinne / Poussin-Courmontagne, Pierre / Voilquin, Laetitia / Eberling, Pascal / Ruffenach, Frank / Cavarelli, Jean / Slee, John / Levine, Timothy P / Drin, Guillaume / Tomasetto, Catherine / Alpy, Fabien

The EMBO journal

2020 Volume 39, Issue 23, Page(s) e104369

Abstract: Organelles are physically connected in membrane contact sites. The endoplasmic reticulum possesses three major receptors, VAP-A, VAP-B, and MOSPD2, which interact with proteins at the surface of other organelles to build contacts. VAP-A, VAP-B, and ... ...

Abstract	Organelles are physically connected in membrane contact sites. The endoplasmic reticulum possesses three major receptors, VAP-A, VAP-B, and MOSPD2, which interact with proteins at the surface of other organelles to build contacts. VAP-A, VAP-B, and MOSPD2 contain an MSP domain, which binds a motif named FFAT (two phenylalanines in an acidic tract). In this study, we identified a non-conventional FFAT motif where a conserved acidic residue is replaced by a serine/threonine. We show that phosphorylation of this serine/threonine is critical for non-conventional FFAT motifs (named Phospho-FFAT) to be recognized by the MSP domain. Moreover, structural analyses of the MSP domain alone or in complex with conventional and Phospho-FFAT peptides revealed new mechanisms of interaction. Based on these new insights, we produced a novel prediction algorithm, which expands the repertoire of candidate proteins with a Phospho-FFAT that are able to create membrane contact sites. Using a prototypical tethering complex made by STARD3 and VAP, we showed that phosphorylation is instrumental for the formation of ER-endosome contacts, and their sterol transfer function. This study reveals that phosphorylation acts as a general switch for inter-organelle contacts.
MeSH term(s)	Amino Acid Motifs ; Binding Sites ; Endoplasmic Reticulum/metabolism ; Endosomes/metabolism ; Humans ; Lipid Metabolism ; Lipids ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Models, Molecular ; Phosphorylation ; Protein Binding ; Receptors, Chemokine/chemistry ; Receptors, Chemokine/genetics ; Receptors, Chemokine/metabolism ; Vesicular Transport Proteins/chemistry ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism
Chemical Substances	Lipids ; MOSPD2 protein, human ; Membrane Proteins ; Receptors, Chemokine ; VAPA protein, human ; VAPB protein, human ; Vesicular Transport Proteins
Language	English
Publishing date	2020-10-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2019104369
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Article ; Online: Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites.

Di Mattia, Thomas / Wilhelm, Léa P / Ikhlef, Souade / Wendling, Corinne / Spehner, Danièle / Nominé, Yves / Giordano, Francesca / Mathelin, Carole / Drin, Guillaume / Tomasetto, Catherine / Alpy, Fabien

EMBO reports

2018 Volume 19, Issue 7

Abstract: Membrane contact sites are cellular structures that mediate interorganelle exchange and communication. The two major tether proteins of the endoplasmic reticulum (ER), VAP-A and VAP-B, interact with proteins from other organelles that possess a small VAP- ...

Abstract	Membrane contact sites are cellular structures that mediate interorganelle exchange and communication. The two major tether proteins of the endoplasmic reticulum (ER), VAP-A and VAP-B, interact with proteins from other organelles that possess a small VAP-interacting motif, named FFAT [two phenylalanines (FF) in an acidic track (AT)]. In this study, using an unbiased proteomic approach, we identify a novel ER tether named motile sperm domain-containing protein 2 (MOSPD2). We show that MOSPD2 possesses a Major Sperm Protein (MSP) domain which binds FFAT motifs and consequently allows membrane tethering
MeSH term(s)	Amino Acid Motifs/genetics ; Animals ; Binding Sites/genetics ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Endosomes/genetics ; Golgi Apparatus/genetics ; Humans ; Male ; Membrane Proteins/genetics ; Mice ; Mitochondrial Membranes/metabolism ; Protein Binding ; Proteomics ; Receptors, Chemokine/genetics ; Spermatozoa/metabolism ; Vesicular Transport Proteins/genetics
Chemical Substances	MOSPD2 protein, human ; Membrane Proteins ; Receptors, Chemokine ; VAPA protein, human ; VAPB protein, human ; Vesicular Transport Proteins
Language	English
Publishing date	2018-06-01
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.201745453
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