MCS.ID	synonyms	gene.ID	gene.symbol	uniprot	species	MCS	location.literature.	cell.line.tissue	Experimental.Method	source.number	PMID-1	Description-1	Evidences-1	PMID-2	Description-2	Evidences-2	PMID-3	Description-3	Evidences-3	PMID-4	Description-4	Evidences-4	PMID-5	Description-5	Evidences-5	PMID-6	Description-6	Evidences-6	PMID-7	Description-7	Evidences-7	PMID-8	Description-8	Evidences-8	PMID-9	Description-9	Evidences-9	PMID-10	Description-10	Evidences-10	PMID-11	Description-11	Evidences-11	PMID-12	Description-12	Evidences-12
LMCS00291	PVA11; VAP27; VAP27-1; At3g60600; T4C21.10	825231	PVA11	Q8VZ95	Arabidopsis thaliana	ER-MT; MT-ER	ER	Arabidopsis	Low throughput experimental methods	1	36163196	ER-mitochondrial contact sites (EMCSs) are important for mitochondrial function. Here, we have identified a EMCS complex, comprising a family of uncharacterised mitochondrial outer membrane proteins, TRB1, TRB2, and the ER protein, VAP27-1.	The protein was validated by immunostaining, live cell imaging, KSP, proteomics screen, co-immunoprecipitation, western blotting, electron microscopy and real-time qPCR in arabidopsis, which regulates ER-mitochondrial interactions and mitophagy.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00398	NET3C; At2g47920; F17A22.31	819404	NET3C	O82259	Arabidopsis thaliana	ER-PM; PM-ER	ER	Arabidopsis	Low throughput experimental methods	2	24909329	The Plant Cytoskeleton, NET3C, and VAP27 Mediate the Link between the Plasma Membrane and Endoplasmic Reticulum.	The protein was validated by live cell imaging, FRET-FLIM, transmission electron microscopy, immune-gold labeling, co-immunoprecipitation assay, western blotting and chi-square analysis in arabidopsis, which links the actin cytoskeleton to ER-PM contact sites.	27159525	The endoplasmic reticulum (ER) is connected to the plasma membrane (PM) through the plant-specific NETWORKED protein, NET3C, and phylogenetically conserved vesicle-associated membrane protein-associated proteins (VAPs).	The protein was validated by confocal microscopy, live cell imaging, transmission electron microscopy and immunogold labelling in arabidopsis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00399	PVA11; VAP27; VAP27-1; At3g60600; T4C21.10	825231	PVA11	Q8VZ95	Arabidopsis thaliana	ER-PM; PM-ER	ER	Arabidopsis	Low throughput experimental methods	5	24909329	The Plant Cytoskeleton, NET3C, and VAP27 Mediate the Link between the Plasma Membrane and Endoplasmic Reticulum.	The protein was validated by live cell imaging, FRET-FLIM, transmission electron microscopy, immune-gold labeling, co-immunoprecipitation assay, western blotting and chi-square analysis in arabidopsis, which is phylogenetically conserved and interacts with NET3C and microtubules.	36252028	Under normal conditions, ORP2A locates to EPCSs and interacts with VAP27-1.	The protein was validated by ET analysis, high-pressure freezing, immunogold-TEM analysis, transient expression in protoplasts and confocal imaging in arabidopsis.	https://doi.org/10.7936/2hqh-f829	I propose a model wherein MSL10’s direct interaction with VAP27s creates EPCSs which has implications for MSL10 function.	The protein was validated by tandem mass spectrometry, mbSUS assay, FRET-FLIM, BiFC, co-localization analysis, hybridization, PCR, immunodetection, immunoblot, trypan blue staining,  and microscope in arabidopsis, which has implications for MSL10 function.	27811083	SYT1 and VAP27-1 were shown to be localized on distinct ER–PM contact sites.	The protein was validated by FRAP analysis, western blot, immunogold labeling, whole-mount immunofluorescence labeling and confocal microscopy in arabidopsis.	27159525	The endoplasmic reticulum (ER) is connected to the plasma membrane (PM) through the plant-specific NETWORKED protein, NET3C, and phylogenetically conserved vesicle-associated membrane protein-associated proteins (VAPs).	The protein was validated by confocal microscopy, live cell imaging, transmission electron microscopy and immunogold labelling in arabidopsis, which used at EPCSs are essential for normal ER–cytoskeleton interaction and for plant development.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00457	SYT1; SYTA; At2g20990; F26H11.25; F5H14.5	816633	SYT1	Q9SKR2	Arabidopsis thaliana	ER-PM; PM-ER	NA	SF9 cells; Arabidopsis	Low throughput experimental methods	6	35451158	The Arabidopsis ER-anchored synaptotagmin 1 (SYT1), enriched in EPCSs, plays a critical role in plant abiotic stress tolerance.	The protein was validated by FRET-based lipid transfer assay, fluorescent lipid transfer assay, liposome tethering assay and liposome coflotation assay in SF9 cells, which mediates lipid transport in a lipid composition-dependent manner.	10.14288/1.0413757	The Arabidopsis SYNAPTOTAGMIN1 (SYT1) EPCS tether.	The protein was validated by bioluminescence assay, histochemical GUS staining and bioinformatic analysis in arabidopsis.	31869440	Synaptotagmin 1 (SYT1) has been recognised as a tethering factor of plant endoplasmic reticulum (ER)–plasma membrane (PM) contact sites (EPCSs) and partially localises to around plasmodesmata (PD).	The protein was validated by immunoprecipitation, mass analysis, confocal microscopy, electron microscopy, RT-PCR, GFP pull-down assay and bioinformatic analysis in arabidopsis.	30126867	SYT1 is specifically localized to the boundary between the ER and PM.	The protein was validated by confocal microscopy and statistical analyses in arabidopsis, and SYT1 deficiency caused a reduction of the immobile tubules and enlargement of the ER meshes.	27811083	Arabidopsis synaptotagmin 1 (SYT1) is localized on the endoplasmic reticulum–plasma membrane (ER–PM) contact sites in leaf and root cells. 	The protein was validated by FRAP analysis, western blot, immunogold labeling, whole-mount immunofluorescence labeling and confocal microscopy in arabidopsis, which maintains stability of cortical endoplasmic reticulum networks and VAP27-1-enriched endoplasmic reticulum–plasma membrane contact sites.	32973839	Ionic stress enhances ER–PM connectivity via phosphoinositide-associated SYT1 contact site expansion in Arabidopsis.	The protein was validated by image acquisition, quantitative analyses and FRAP experiments in arabidopsis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00460	At1g07985	2745747	At1g07985	Q3EDG6	Arabidopsis thaliana	LD-PM; PM-LD	ER	Thaliana plants	Low throughput experimental methods	1	35348751	Here, we identified and characterized three proteins of Arabidopsis thaliana that form a lipid droplet (LD)–plasma membrane (PM) tethering complex in plant cells, namely LD-localized SEED LD PROTEIN (SLDP) 1 and SLDP2 and PM-localized LD-PLASMA MEMBRANE ADAPTOR (LIPA).	The protein was validated by stable transformation, RNA isolation, qPCR, particle bombardment, pollen tube microscopy, CLSM-based FLIM-FRET analysis, Y2H, proteomic analysis, electron microscopy and bioinformatics in thaliana plants.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00511	MIRO2; At3g63150; T20O10.250	825490	MIRO2	F4J0W4	Arabidopsis thaliana	ER-MT; MT-ER	NA	Tobacco leaf epidermal cells	Low throughput experimental methods	1	32246085	Here, we show a role for the GTPase Miro2 in mitochondria interaction with the ER and its impacts on mitochondria fusion and motility.	The protein was validated by spinning disc confocal imaging, optical trapping setup, data generation and analysis in tobacco leaf epidermal cells, which promotes mitochondrial fusion.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00531	ORP2A; At4g22540; F7K2.120	828349	ORP2A	Q940Y1	Arabidopsis thaliana	ER-PM; PM-ER	ER	Arabidopsis	Low throughput experimental methods	1	36252028	Under normal conditions, ORP2A locates to EPCSs and interacts with VAP27-1.	The protein was validated by ET analysis, high-pressure freezing, immunogold-TEM analysis, transient expression in protoplasts and confocal imaging in arabidopsis, which regulates PI3P in plant autophagy.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00532	ORP2A; At4g22540; F7K2.120	828349	ORP2A	Q940Y1	Arabidopsis thaliana	ER-Autophagosome; Autophagosome-ER	ER	Arabidopsis	Low throughput experimental methods	1	36252028	However, upon autophagic induction, ORP2A interacts with VAP27-1 and ATG8e as a complex to bridge the EACSs.	The protein was validated by ET analysis, high-pressure freezing, immunogold-TEM analysis, transient expression in protoplasts and confocal imaging in arabidopsis, which regulates PI3P in plant autophagy.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00533	PVA11; VAP27; VAP27-1; At3g60600; T4C21.10	825231	PVA11	Q8VZ95	Arabidopsis thaliana	ER-Autophagosome; Autophagosome-ER	ER	Arabidopsis	Low throughput experimental methods	1	36252028	However, upon autophagic induction, ORP2A interacts with VAP27-1 and ATG8e as a complex to bridge the EACSs.	The protein was validated by ET analysis, high-pressure freezing, immunogold-TEM analysis, transient expression in protoplasts and confocal imaging in arabidopsis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00534	ATG8E; APG8E; At2g45170; F4L23; T14P1.2	819125	ATG8E	Q8S926	Arabidopsis thaliana	ER-Autophagosome; Autophagosome-ER	Autophagosome	Arabidopsis	Low throughput experimental methods	1	36252028	However, upon autophagic induction, ORP2A interacts with VAP27-1 and ATG8e as a complex to bridge the EACSs.	The protein was validated by ET analysis, high-pressure freezing, immunogold-TEM analysis, transient expression in protoplasts and confocal imaging in arabidopsis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00535	TRB2; TBP3; At5g67580; K9I9.15	836894	TRB2	Q9FJW5	Arabidopsis thaliana	ER-MT; MT-ER	ER; MT	Arabidopsis	Low throughput experimental methods	1	36163196	ER-mitochondrial contact sites (EMCSs) are important for mitochondrial function. Here, we have identified a EMCS complex, comprising a family of uncharacterised mitochondrial outer membrane proteins, TRB1, TRB2, and the ER protein, VAP27-1.	The protein was validated by immunostaining, live cell imaging, KSP, proteomics screen, co-immunoprecipitation, western blotting, electron microscopy and real-time qPCR in arabidopsis, which regulates ER-mitochondrial interactions and mitophagy.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00536	TRB1; At1g49950; F2J10.16	841418	TRB1	Q8VWK4	Arabidopsis thaliana	ER-MT; MT-ER	MT	Arabidopsis	Low throughput experimental methods	1	36163196	ER-mitochondrial contact sites (EMCSs) are important for mitochondrial function. Here, we have identified a EMCS complex, comprising a family of uncharacterised mitochondrial outer membrane proteins, TRB1, TRB2, and the ER protein, VAP27-1.	The protein was validated by immunostaining, live cell imaging, KSP, proteomics screen, co-immunoprecipitation, western blotting, electron microscopy and real-time qPCR in arabidopsis, which regulates ER-mitochondrial interactions and mitophagy.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00576	MSL10; At5g12080; F14F18.230; MXC9.3	831081	MSL10	Q9LYG9	Arabidopsis thaliana	ER-PM; PM-ER	PM	Arabidopsis	Low throughput experimental methods	1	https://doi.org/10.7936/2hqh-f829	Both screens unexpectedly implicated ER-plasma membrane contact sites (EPCSs) in MSL10 function.	The protein was validated by tandem mass spectrometry, mbSUS assay, FRET-FLIM, BiFC, co-localization analysis, hybridization, PCR, immunodetection, immunoblot, trypan blue staining,  and microscope in arabidopsis, which provides new insight into the function and regulation of this type of subcellular compartment.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00577	PVA12; VAP12; At2g45140; T14P1.5	819122	PVA12	Q9SHC8	Arabidopsis thaliana	ER-PM; PM-ER	PM	Arabidopsis	Low throughput experimental methods	1	https://doi.org/10.7936/2hqh-f829	I propose a model wherein MSL10’s direct interaction with VAP27s creates EPCSs which has implications for MSL10 function.	The protein was validated by tandem mass spectrometry, mbSUS assay, FRET-FLIM, BiFC, co-localization analysis, hybridization, PCR, immunodetection, immunoblot, trypan blue staining,  and microscope in arabidopsis, which has implications for MSL10 function.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00613	LIP1; LPLA; At2g20860; F5H14.17	816619	LIP1	Q9ZWT1	Arabidopsis thaliana	LD-PM; PM-LD	PM	Arabidopsis	Low throughput experimental methods	1	10.1101/2022.01.13.476213	SLDP and LIPA mediate lipid droplet-plasma membrane tethering in Arabidopsis thaliana.	The protein was validated by CRISPR/Cas9, qPCR, FLIM-FRET analysis, yeast two-hybrid, proteomic analysis, electron microscopy and bioinformatics in arabidopsis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00614	SMP1; At3g12960; MGH6.8	842817	sldp1	F4I9U3	Arabidopsis thaliana	LD-PM; PM-LD	LD	Arabidopsis	Low throughput experimental methods	1	10.1101/2022.01.13.476213	SLDP and LIPA mediate lipid droplet-plasma membrane tethering in Arabidopsis thaliana.	The protein was validated by CRISPR/Cas9, qPCR, FLIM-FRET analysis, yeast two-hybrid, proteomic analysis, electron microscopy and bioinformatics in arabidopsis.	35348751	Here, we identified and characterized three proteins of Arabidopsis thaliana that form a lipid droplet (LD)–plasma membrane (PM) tethering complex in plant cells, namely LD-localized SEED LD PROTEIN (SLDP) 1 and SLDP2 and PM-localized LD-PLASMA MEMBRANE ADAPTOR (LIPA).	The protein was validated by stable transformation, RNA isolation, qPCR, particle bombardment, pollen tube microscopy, CLSM-based FLIM-FRET analysis, Y2H, proteomic analysis, electron microscopy and bioinformatics in thaliana plants.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00615	AXX17_At5g36100	NA	sldp2	A0A178UK34	Arabidopsis thaliana	LD-PM; PM-LD	LD	Arabidopsis	Low throughput experimental methods	1	10.1101/2022.01.13.476213	SLDP and LIPA mediate lipid droplet-plasma membrane tethering in Arabidopsis thaliana.	The protein was validated by CRISPR/Cas9, qPCR, FLIM-FRET analysis, yeast two-hybrid, proteomic analysis, electron microscopy and bioinformatics in arabidopsis.	35348751	Here, we identified and characterized three proteins of Arabidopsis thaliana that form a lipid droplet (LD)–plasma membrane (PM) tethering complex in plant cells, namely LD-localized SEED LD PROTEIN (SLDP) 1 and SLDP2 and PM-localized LD-PLASMA MEMBRANE ADAPTOR (LIPA).	The protein was validated by stable transformation, RNA isolation, qPCR, particle bombardment, pollen tube microscopy, CLSM-based FLIM-FRET analysis, Y2H, proteomic analysis, electron microscopy and bioinformatics in thaliana plants.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA