MCS_ID Uniprot symbol synonyms gene_ID (entrez) Species MCS location (literature) cell.line.tissue Experimental.Method PMID Description Evidences complex_ID complex LMCS00107 O54902 Slc11a2 Slc11a2; Dct1; Dmt1; Nramp2 25715 Rat ER-Endosome; Endosome-ER MT Rat renal cortex Low throughput experimental methods 29317744 Nevertheless, it is attractive to speculate that endosomal DMT1 interacting with OMM DMT1 contributes not only to the docking but also provides a source of protons to drive the process. The protein was validated by metal transport assays, radioisotope tracers, PGSK fluorescence, immunoblotting and protein determination in rat renal cortex, which have a role in mitochondrial Fe2+ and Mn2+ acquisition. LMCS00108 D4A1W8 Mttp Mttp; Mtp 310900 Rat ER-MT; MT-ER ER Rat livers Low throughput experimental methods 7961664 In addition, the microsomal triacylglycerol transfer protein, which is required for the assembly secretion of apolipoprotein B-containing lipoproteins, was present in the MAM. The protein was validated by immunocytochemistry, electron microscopy and conventional electron microscopy in rat livers. LMCS00111 C0HLN0 Pigbos1 Pigbos1 100909598 Rat ER-MT; MT-ER MT Rat C6 cells; Rat tissues Low throughput experimental methods 31653868 This result demonstrated that the PIGBOS-CLCC1 interaction can be regulated by modulation of ER-mitochondria contacts, and further bolstered the model of CLCC1 and PIGBOS interacting at ER-mitochondria contact sites. The protein was validated by confocal imaging, APEX labeling in live cells, immunoprecipitations, flow cytometry analysis, western blot analysisand EM in rat C6 cells and rat tissues, and the loss of PIGBOS leads to heightened UPR and increased cell death. CMCS00176 Pigbos1_Clcc1 LMCS00112 Q9WU61 Clcc1 Clcc1; Mclc 170927 Rat ER-MT; MT-ER ER Rat C6 cells; Rat tissues Low throughput experimental methods 31653868 This result demonstrated that the PIGBOS-CLCC1 interaction can be regulated by modulation of ER-mitochondria contacts, and further bolstered the model of CLCC1 and PIGBOS interacting at ER-mitochondria contact sites. The protein was validated by confocal imaging, APEX labeling in live cells, immunoprecipitations, flow cytometry analysis and EM in HEK293 cells, HEK293T cells, U2-OS cells, COS-7 cells and HeLa cells, and the loss of PIGBOS leads to heightened UPR and increased cell death. CMCS00176 Pigbos1_Clcc1 LMCS00113 A0A0G2K437 Amfr Amfr 267 Rat ER-MT; MT-ER NA Rat livers; MDCK II cells Low throughput experimental methods 10995452 By EM, smooth ER AMF-R tubules exhibit direct interactions with Mitochondrion. The protein was validated by confocal and electron microscopy in rat livers and MDCK II cells. LMCS00121 P48721 Hspa9 Hspa9; Grp75; Hspa9a 291671 Rat ER-MT; MT-ER MT Rat livers Low throughput experimental methods 17178908 VDAC1, grp75, and IP3Rs are present in a macromolecular complex at the ER-mitochondria interface. The protein was validated by subcellular fractionation, proteomic analysis, targeted aequorin probes and Imaging techniques in rat livers, which directly enhanced Ca2+ accumulation in mitochondria. CMCS00065 Vdac1_Itpr3_Hspa9 LMCS00122 Q9Z2L0 Vdac1 Vdac1 83529 Rat ER-MT; MT-ER MT Rat livers Low throughput experimental methods 17178908 VDAC1, grp75, and IP3Rs are present in a macromolecular complex at the ER-mitochondria interface. The protein was validated by subcellular fractionation, proteomic analysis, targeted aequorin probes and Imaging techniques in rat livers, which directly enhanced Ca2+ accumulation in mitochondria. CMCS00065 Vdac1_Itpr3_Hspa9 LMCS00130 P37377 Snca Snca 29219 Rat ER-MT; MT-ER NA Rat cortical neurons; Rat brains Low throughput experimental methods 28337542 alpha-Synuclein is a MAM protein and binds to VAPB but not PTPIP51 in immunoprecipitation assays. The protein was validated by SDS-PAGE, immunoblotting, immunoprecipitation and GST pull-down assays, biochemical fractionation and microscopy in rat cortical neuronsand rat brains, which disrupts Ca2+ homeostasis and mitochondrial ATP production. CMCS00174 Vapb_Snca LMCS00159 Q66H15 Rmdn3 Rmdn3; Fam82a2; Fam82c; Ptpip51 311328 Rat ER-MT; MT-ER MT Hippocampal neurons; Rat cortical neurons; Rat brains Low throughput experimental methods 30841933__28337542__35090998 The VAPB-PTPIP51 endoplasmic reticulum-mitochondria tethering proteins are present in neuronal synapses and regulate synaptic activity__However, many neuronal functions damaged in Parkinson’s disease are regulated by signalling between the endoplasmic reticulum (ER) and mitochondria. This signalling involves close physical associations between the two organelles that are mediated by binding of the integral ER protein vesicle-associated membrane protein-associated protein B (VAPB) to the outer mitochondrial membrane protein, protein tyrosine phosphatase-interacting protein 51 (PTPIP51). VAPB and PTPIP51 thus act as a scaffold to tether the two organelles.__Lanthanum decreased VAPB-PTPP51, BAP31-FIS1, and MFN2-MFN1 expression of mitochondria-associated membranes and induced abnormal autophagy in rat hippocampus. The protein was validated by protein fractionation, SDS–PAGE, immunoblotting,immunofluorescence staining, proximity ligation assays and microscopy in hippocampal neurons, and the results reveal a new role for the VAPB-PTPIP51 tethers in neurons and suggest that damage to ER-Mitochondrion signaling contributes to synaptic dysfunction in Parkinson's disease and FTD or ALS..__The protein was validated by SDS-PAGE, immunoblotting, immunoprecipitation and GST pull-down assays, biochemical fractionation and microscopy in rat cortical neuronsand, rat brains, and alpha-Synuclein binds to the ER–mitochondria tethering protein VAPB to disrupt Ca2+ homeostasis and mitochondrial ATP production.__The protein was validated by morris water maze, transmission electron microscopy, nissl staining, immunofluorescence test , real-time quantitative PCR and western blot analysis in rat hippocampal cells and tissues. CMCS00084 Vapb_Rmdn3 LMCS00160 Q9Z269 Vapb Vapb 60431 Rat ER-MT; MT-ER ER Hippocampal neurons; Rat cortical neurons; Rat brains Low throughput experimental methods 30841933__28337542__35090998 Here, we demonstrate that the VAPB-PTPIP51 tethers regulate synaptic activity.VAPB and PTPIP51 localise and form contacts at synapses, and stimulating neuronal activity increases ER-Mitochondrion contacts and the VAPB-PTPIP51 interaction.Moreover, siRNA loss of VAPB or PTPIP51 perturbs synaptic function and dendritic spine morphology.Our results reveal a new role for the VAPB-PTPIP51 tethers in neurons and suggest that damage to ER-Mitochondrion signaling contributes to synaptic dysfunction in Parkinson's disease and FTD or ALS.__alpha-Synuclein is a MAM protein and binds to VAPB but not PTPIP51 in immunoprecipitation assays.__Lanthanum decreased VAPB-PTPP51, BAP31-FIS1, and MFN2-MFN1 expression of mitochondria-associated membranes and induced abnormal autophagy in rat hippocampus. The protein was validated by protein fractionation, SDS–PAGE, immunoblotting,immunofluorescence staining, proximity ligation assays and microscopy in hippocampal neurons, and the results reveal a new role for the VAPB-PTPIP51 tethers in neurons and suggest that damage to ER-Mitochondrion signaling contributes to synaptic dysfunction in Parkinson's disease and FTD or ALS..__The protein was validated by SDS-PAGE, immunoblotting, immunoprecipitation and GST pull-down assays, biochemical fractionation and microscopy in rat cortical neuronsand, rat brains, and alpha-Synuclein binds to the ER–mitochondria tethering protein VAPB to disrupt Ca2+ homeostasis and mitochondrial ATP production.__The protein was validated by morris water maze, transmission electron microscopy, nissl staining, immunofluorescence test , real-time quantitative PCR and western blot analysis in rat hippocampal cells and tissues. CMCS00084/CMCS00174 Vapb_Rmdn3/Vapb_Snca LMCS00161 P60571 Panx2 Panx2; Px2 362979 Rat ER-MT; MT-ER ER C6 glioma cells Low throughput experimental methods 30862038 Pannexin 2 localizes at ER-Mitochondria contact sites. The protein was validated by live-cell imaging, panx2 trajectory analysis, immunofluorescence, co-Localization analysis, pre-pmbedding immunoelectron microscopy and western blotting in C6 glioma cells, which sensitizes cells to apoptotic stimuli. LMCS00169 P84817 Fis1 Fis1; Ttc11 288584 Rat ER-MT; MT-ER MT Rat hippocampal cells and tissues Low throughput experimental methods 35090998 Lanthanum decreased VAPB-PTPP51, BAP31-FIS1, and MFN2-MFN1 expression of mitochondria-associated membranes and induced abnormal autophagy in rat hippocampus. The protein was validated by morris water maze, transmission electron microscopy, nissl staining, immunofluorescence test , real-time quantitative PCR and western blot analysis in rat hippocampal cells and tissues. CMCS00088 Bcap31_Fis1 LMCS00170 Q6AY58 Bcap31 Bcap31 293852 Rat ER-MT; MT-ER ER Rat hippocampal cells and tissues Low throughput experimental methods 35090998 Lanthanum decreased VAPB-PTPP51, BAP31-FIS1, and MFN2-MFN1 expression of mitochondria-associated membranes and induced abnormal autophagy in rat hippocampus. The protein was validated by morris water maze, transmission electron microscopy, nissl staining, immunofluorescence test , real-time quantitative PCR and western blot analysis in rat hippocampal cells and tissues. CMCS00088 Bcap31_Fis1 LMCS00171 O35547 Acsl4 Acsl4; Acs4; Facl4 113976 Rat ER-MT; MT-ER ER; MT Rat livers Low throughput experimental methods 11319232__12147264 We have previously shown that in rat liver, ACS1 is located in ER, mitochondrial-associated membrane (MAM), and cytosol, ACS4 is located in MAM.__Rat liver acyl-CoA synthetase 4 is a peripheral-membrane protein located in two distinct subcellular organelles, peroxisomes, and Mitochondrionl-associated membrane. The protein was validated by immunoblotting and immunoblotting in rat livers, which may be linked to triacylglycerol synthesis.__The protein was validated by northern analyses, immunoblotting and enzyme assays in rat livers, which is probably targeted and linked to MAM and peroxisomes by interactions with other proteins. LMCS00172 P18163 Acsl1 Acsl1; Acs1; Acsl2; Facl2 25288 Rat ER-MT; MT-ER ER Rat livers Low throughput experimental methods 11319232__12147264 We have previously shown that in rat liver, ACS1 is located in ER, mitochondrial-associated membrane (MAM), and cytosol, ACS4 is located in MAM.__ACS1 had been localized to three different subcellular regions in rat liver, endoplasmic reticulum, Mitochondrion, and peroxisomes. The protein was validated by immunoblotting and immunoblotting in rat livers, which may be linked to triacylglycerol synthesis.__The protein was validated by northern analyses, immunoblotting and enzyme assays in rat livers. LMCS00175 Q63269 Itpr3 Itpr3 25679 Rat ER-MT; MT-ER ER Rat livers Low throughput experimental methods 17178908 VDAC1, grp75, and IP3Rs are present in a macromolecular complex at the ER-mitochondria interface. The protein was validated by subcellular fractionation, proteomic analysis, targeted aequorin probes and Imaging techniques in rat livers, which directly enhanced Ca2+ accumulation in mitochondria. CMCS00065 Vdac1_Itpr3_Hspa9 LMCS00210 P09527 Rab7a Rab7a; Rab7 29448 Rat ER-Endosome; Endosome-ER Endosome PC12 cells Low throughput experimental methods 25855459 Such fusion induces outgrowth of protrusions and neurites, which requires the abilities of protrudin and FYCO1 to interact with LEs and kinesin 1.Thus, protrudin-containing ER-LE contact sites are platforms for kinesin-1 loading onto LEs, and kinesin-1-mediated translocation of LEs to the plasma membrane, fuelled by repeated ER contacts, promotes protrusion and neurite outgrowth. The protein was validated by microscopy, siRNA experiments, GFP-trap assay in PC12 cells, and these results correlate strongly with the cooperative effects of protrudin and FYCO1 in protrusion and neurite outgrowth. CMCS00010 ZFYVE27_Fyco1_Kif5b_Rab7a_PI(3)P LMCS00211 Q6P7B7 Zfyve27 Zfyve27; Protrudin 309376 Rat ER-Endosome; Endosome-ER ER PC12 cells Low throughput experimental methods 25855459 Such fusion induces outgrowth of protrusions and neurites, which requires the abilities of protrudin and FYCO1 to interact with LEs and kinesin 1.Thus, protrudin-containing ER-LE contact sites are platforms for kinesin-1 loading onto LEs, and kinesin-1-mediated translocation of LEs to the plasma membrane, fuelled by repeated ER contacts, promotes protrusion and neurite outgrowth. The protein was validated by microscopy, siRNA experiments, GFP-trap assay in PC12 cells, and these results correlate strongly with the cooperative effects of protrudin and FYCO1 in protrusion and neurite outgrowth. CMCS00010 ZFYVE27_Fyco1_Kif5b_Rab7a_PI(3)P LMCS00235 Q5FVP8 Dgat2 Dgat2 252900 Rat ER-MT; MT-ER ER Rat livers; McArdle-RH7777 rat hepatoma cells Low throughput experimental methods 7961664__19049983 Specific activities of diacylglycerol acyltransferase, acyl-coen- zyme Acholesterol acyltransferase, and phosphatidyl- serine synthase (base exchange enzyme) are enriched 2.2-3.4-fold in the MAM compared with endoplasmic re- ticulum. __The endoplasmic reticulum enzyme DGAT2 Is found in mitochondrion-associated membranes and has a mitochondrionl targeting signal that promotes its association with mitochondrion. The protein was validated by immunocytochemistry, electron microscopy and conventional electron microscopy in rat livers.__The protein was validated by immunoblot analyses and immunofluorescence microscopy in McArdle-RH7777 rat hepatoma cells, which N terminus may promote its association with mitochondria. LMCS00339 M0R7Z9 Plin5 Plin5; Lsdp5; Oxpat 501283 Rat MT-LD; LD-MT LD; MT Cardiac myocytes Low throughput experimental methods 21885430 Perilipin 5, a lipid droplet-associated protein, provides physical and metabolic linkage to Mitochondrion. The protein was validated by EM, micrograph analysis, immunoblot analysis, beta-oxidation measurements and statistical analysis in cardiac myocytes, which provides physical and metabolic linkage to mitochondria. LMCS00384 Q9Z270 Vapa Vapa; Vap33 58857 Rat ER-Transport vesicle; Transport vesicle-ER ER L6 cell; 3T3-L1 cells Low throughput experimental methods 11208137 A functional role for VAP-33 in insulin-stimulated GLUT4 traffic. The protein was validated by western blotting, immunocytochemistry and microinjection/lawn assay in L6 cell and 3T3-L1 cells, and this model may be instructive for understanding the pathogenesis of HSP diseases, which may be a regulator of VAMP-2 availability for GLUT4 traffic and other vesicle fusion events. LMCS00395 Q9ES21 Sacm1l Sacm1l; Sac1 116482 Rat ER-PM; PM-ER ER SCG neurons Low throughput experimental methods 27044890 Thus, the dynamic presence of Sac1 at ER-PM contact sites allows it to act as a cellular sensor and controller of PM phosphoinositides, thereby influencing many PM processes. The protein was validated by fluorescence microscopy, UHPLC/MS, patch-clamp recordings and photometric FRET measurements in SCG neurons, and the dynamic presence of Sac1 at ER–PM contact sites allows it to act as a cellular sensor and controller of PM phosphoinositides, thereby influencing many PM processes. LMCS00416 O54902 Slc11a2 Slc11a2; Dct1; Dmt1; Nramp2 25715 Rat MT-LY; LY-MT MT Rat kidney PT cells Low throughput experimental methods 24448823 We suggest that DMT1 not only exports iron from endosomes, but also serves to import the metal into the mitochondria. The protein was validated by split-ubiquitin yeast 2-hybrid analysis, coimmunoprecipitation, immunofluorescence microscopy and immunogold electron microscopy in rat kidney PT cells. LMCS00417 Q2PQA9 Kif5b Kif5b; Khc 117550 Rat ER-Endosome; Endosome-ER Endosome PC12 cells Low throughput experimental methods 25855459 Here we show in human and rat cell lines that protrudin, an ER protein that promotes protrusion and neurite outgrowth, forms contact sites with late endosomes (LEs) via coincident detection of the small GTPase RAB7 and phosphatidylinositol 3-phosphate (PtdIns(3)P). These contact sites mediate transfer of the microtubule motor kinesin 1 from protrudin to the motor adaptor FYCO1 on LEs. The protein was validated by microscopy, siRNA experiments, GFP-trap assay in PC12 cells, and these results correlate strongly with the cooperative effects of protrudin and FYCO1 in protrusion and neurite outgrowth. CMCS00010 ZFYVE27_Fyco1_Kif5b_Rab7a_PI(3)P LMCS00427 Q8R500 Mfn2 Mfn2; Fzo1a 64476 Rat ER-MT; MT-ER MT Rat hippocampal cells and tissues Low throughput experimental methods 35090998 Lanthanum decreased VAPB-PTPP51, BAP31-FIS1, and MFN2-MFN1 expression of mitochondria-associated membranes and induced abnormal autophagy in rat hippocampus. The protein was validated by morris water maze, transmission electron microscopy, nissl staining, immunofluorescence test , real-time quantitative PCR and western blot analysis in rat hippocampal cells and tissues. CMCS00085 Mfn2_Mfn1 LMCS00428 Q8R4Z9 Mfn1 Mfn1; Fzo1b 192647 Rat ER-MT; MT-ER MT Rat hippocampal cells and tissues Low throughput experimental methods 35090998 Lanthanum decreased VAPB-PTPP51, BAP31-FIS1, and MFN2-MFN1 expression of mitochondria-associated membranes and induced abnormal autophagy in rat hippocampus. The protein was validated by morris water maze, transmission electron microscopy, nissl staining, immunofluorescence test , real-time quantitative PCR and western blot analysis in rat hippocampal cells and tissues. CMCS00085 Mfn2_Mfn1 LMCS00499 P15387 Kcnb1 Kcnb1 25736 Rat ER-PM; PM-ER PM Rat hippocampal neurons Low throughput experimental methods 30012696__29941597 Multiplex immunolabeling revealed colocalization of Kv2.1 and Kv2.2 with endogenous VAPs at ER-PM junctions in brain neurons from male and female mice in situ and in cultured rat hippocampal neurons, and KO of VAPA in mammalian cells reduces Kv2.1 clustering.__Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB. The protein was validated by multiplex immunolabeling in rat hippocampal neurons, live-cell tirf imaging and the Kv2.1 expression in the PM can affect ER-PM junctions via its phosphorylation-dependent association to ER-localized VAPA and VAPB.__The protein was validated by immunostaining in rat hippocampal neurons, live-cell tirf imaging and the Kv2-induced ER remodeling and VAP concentration at ER/PM contacts likely play a central role in neuronal physiology. CMCS00195 Kcnb1_Vapa_Vapb LMCS00500 Q63099 Kcnb2 Kcnb2 117105 Rat ER-PM; PM-ER PM Rat hippocampal neurons Low throughput experimental methods 30012696__29941597 Multiplex immunolabeling revealed colocalization of Kv2.1 and Kv2.2 with endogenous VAPs at ER-PM junctions in brain neurons from male and female mice in situ and in cultured rat hippocampal neurons, and KO of VAPA in mammalian cells reduces Kv2.1 clustering.__Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB. The protein was validated by multiplex immunolabeling in rat hippocampal neurons, live-cell tirf imaging and the Kv2.1 expression in the PM can affect ER-PM junctions via its phosphorylation-dependent association to ER-localized VAPA and VAPB.__The protein was validated by immunostaining in rat hippocampal neurons, live-cell tirf imaging and the Kv2-induced ER remodeling and VAP concentration at ER/PM contacts likely play a central role in neuronal physiology. CMCS00196 Kcnb2_Vapa_Vapb LMCS00505 Q9Z270 Vapa Vapa; Vap33 58857 Rat ER-PM; PM-ER ER Rat hippocampal neurons; Primary hippocampal neuron; HEK293T cells Low throughput experimental methods 30012696__29941597__36769244 Multiplex immunolabeling revealed colocalization of Kv2.1 and Kv2.2 with endogenous VAPs at ER-PM junctions in brain neurons from male and female mice in situ and in cultured rat hippocampal neurons, and KO of VAPA in mammalian cells reduces Kv2.1 clustering.__Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB.__Importantly, we demonstrate that proNRG2 promotes the formation of ER-PM junctions by directly binding the ER-resident membrane tether VAP, like Kv2.1. The protein was validated by multiplex immunolabeling in rat hippocampal neurons, live-cell tirf imaging and the Kv2.1 expression in the PM can affect ER-PM junctions via its phosphorylation-dependent association to ER-localized VAPA and VAPB.__The protein was validated by immunostaining in rat hippocampal neurons, live-cell tirf imaging and the Kv2-induced ER remodeling and VAP concentration at ER/PM contacts likely play a central role in neuronal physiology.__The protein was validated by shRNA-mediated knockdown, immunocytochemistry, confocal microscopy, immunogold electron microscopy, immunoprecipitation, GST pulldown assays and western blotting in primary hippocampal neuron. ProNRG2 and Kv2.1 serve as co-regulated downstream effectors of NMDA receptors to homeostatically regulate GABAergic interneurons. CMCS00195/CMCS00196/CMCS00228 Kcnb1_Vapa_Vapb/Kcnb2_Vapa_Vapb/Nrg2_Vapa_Vapb LMCS00506 Q9Z269 Vapb Vapb 60431 Rat ER-PM; PM-ER ER Rat hippocampal neurons; Primary hippocampal neuron; HEK293T cells Low throughput experimental methods 30012696__29941597__36769244 Multiplex immunolabeling revealed colocalization of Kv2.1 and Kv2.2 with endogenous VAPs at ER-PM junctions in brain neurons from male and female mice in situ and in cultured rat hippocampal neurons, and KO of VAPA in mammalian cells reduces Kv2.1 clustering.__Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB.__Importantly, we demonstrate that proNRG2 promotes the formation of ER-PM junctions by directly binding the ER-resident membrane tether VAP, like Kv2.1. The protein was validated by multiplex immunolabeling in rat hippocampal neurons, live-cell tirf imaging and the Kv2.1 expression in the PM can affect ER-PM junctions via its phosphorylation-dependent association to ER-localized VAPA and VAPB.__The protein was validated by immunostaining in rat hippocampal neurons, live-cell tirf imaging and the Kv2-induced ER remodeling and VAP concentration at ER/PM contacts likely play a central role in neuronal physiology.__The protein was validated by shRNA-mediated knockdown, immunocytochemistry, confocal microscopy, immunogold electron microscopy, immunoprecipitation, GST pulldown assays and western blotting in primary hippocampal neuron. ProNRG2 and Kv2.1 serve as co-regulated downstream effectors of NMDA receptors to homeostatically regulate GABAergic interneurons. CMCS00195/CMCS00196/CMCS00228 Kcnb1_Vapa_Vapb/Kcnb2_Vapa_Vapb/Nrg2_Vapa_Vapb LMCS00510 Q9R0C9 Sigmar1 Sigmar1; Oprs1 29336 Rat ER-MT; MT-ER ER Microglial cells Low throughput experimental methods 34601668 Sigma-1R (σ-1R) localizes to the mitochondria-associated membranes (MAMs) and regulates endoplasmic reticulum (ER) and mitochondria communication, in part through its chaperone activity. The protein was validated by TEM, flow cytometry analysis, immunofuorescent staining, confocal microscopic imaging, western blot and Real‑Time RT‑PCR in microglial cells, which suppresses microglia M1 polarization and neuroinfammation via regulating endoplasmic reticulum–mitochondria contact and mitochondrial functions in stress-induced hypertension rats. LMCS00525 Q924S5 Lonp1 Lonp1; Lon; Prss15 170916 Rat ER-MT; MT-ER MT H9C2 cells Low throughput experimental methods 37333972 In the present study, we first identify LonP2 as a new MAM-localized protein that links ER and mitochondria in the cardiomyocytes. The protein was validated by staining, transmission electron microscopy, western blot analysis and fluorescence detection in H9C2 cells, and LonP1 deficiency in the heart results in aberrant metabolic reprogramming and pathological heart remodeling and eventually progresses to heart failure. LMCS00557 Q5BJS4 Fundc1 Fundc1 363442 Rat ER-MT; MT-ER MT H9C2 cells Low throughput experimental methods 35118141 More importantly, we found STAT3-knockdown suppressed LPS-induced expression of FUNDC1, a protein located in mitochondria-associated endoplasmic reticulum membranes (MAMs). The protein was validated by cell viability assay, immunofluorescence staining, transfection, assessment of ROS in H9C2 cells, and IL-6/STAT3 pathway plays a key role in LPS-induced myocardial dysfunction, through regulating the FUNDC1-associated MAMs formation and interfering the function of ER and mitochondria. LMCS00578 O35569 Nrg2 Nrg2; Ntak 432361 Rat ER-PM; PM-ER PM Primary hippocampal neuron Low throughput experimental methods 36769244 Importantly, we demonstrate that proNRG2 promotes the formation of ER-PM junctions by directly binding the ER-resident membrane tether VAP, like Kv2.1. The protein was validated by shRNA-mediated knockdown, immunocytochemistry, confocal microscopy, immunogold electron microscopy, immunoprecipitation, GST pulldown assays and western blotting in primary hippocampal neuron. ProNRG2 and Kv2.1 serve as co-regulated downstream effectors of NMDA receptors to homeostatically regulate GABAergic interneurons. CMCS00228 Nrg2_Vapa_Vapb LMCS00588 D3ZXY2 Pdzd8 Pdzd8 308000 Rat ER-Endosome; Endosome-ER NA PC12 cells Low throughput experimental methods 33912962 PDZD8-mediated lipid transfer at contacts between the ER and late endosomes/lysosomes is required for neurite outgrowth. The protein was validated by confocal microscopy, live cell super-resolution Lattice-SIM microscopy, immunofluorescence staining, quantitative RT-PCR, GFP-trap assay, mass spectrometry, pulldown assays and pull-down assay in PC12 cells, which is required for LE/lys positioning and neurite outgrowth, which is dependent on the lipid transfer activity of the SMP domain. LMCS00589 D3ZXY2 Pdzd8 Pdzd8 308000 Rat ER-LY; LY-ER NA PC12 cells Low throughput experimental methods 33912962 PDZD8-mediated lipid transfer at contacts between the ER and late endosomes/lysosomes is required for neurite outgrowth. The protein was validated by confocal microscopy, live cell super-resolution Lattice-SIM microscopy, immunofluorescence staining, quantitative RT-PCR, GFP-trap assay, mass spectrometry, pulldown assays and pull-down assay in PC12 cells, which is required for LE/lys positioning and neurite outgrowth, which is dependent on the lipid transfer activity of the SMP domain. LMCS00632 D3Z9D2 Fyco1 Fyco1 301085 Rat ER-Endosome; Endosome-ER Endosome PC12 cells Low throughput experimental methods 25855459 Here we show in human and rat cell lines that protrudin, an ER protein that promotes protrusion and neurite outgrowth, forms contact sites with late endosomes (LEs) via coincident detection of the small GTPase RAB7 and phosphatidylinositol 3-phosphate (PtdIns(3)P). These contact sites mediate transfer of the microtubule motor kinesin 1 from protrudin to the motor adaptor FYCO1 on LEs. The protein was validated by microscopy, siRNA experiments, GFP-trap assay in PC12 cells, and these results correlate strongly with the cooperative effects of protrudin and FYCO1 in protrusion and neurite outgrowth. CMCS00010 ZFYVE27_Fyco1_Kif5b_Rab7a_PI(3)P