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UnknownFFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts.
Not available
S-EPMC7705450 | biostudies-literature
ProteomicsHuman VAPome Analysis Reveals MOSPD1 and MOSPD3 as Membrane Contact Site Proteins Interacting with FFAT-Related FFNT Motifs
Membrane contact sites (MCS) are intracellular regions where two organelles come closer to exchange information and material. The majority of the endoplasmic reticulum (ER) MCS are attributed to the ER-localized tether proteins VAPA, VAPB, and MOSPD2. These recruit other proteins to the ER by intera...
ORGANISM(S): Homo sapiens (Human) 
2023-06-29 | PXD043399 | Pride
Emery-dreifuss muscular dystrophy  ffat  ffnt  mospd1  mospd2  mospd3  vapa  vapb  endoplasmic reticulum  membrane contact sites 
UnknownRegulating peroxisome-ER contacts via the ACBD5-VAPB tether by FFAT motif phosphorylation and GSK3β.
Not available
S-EPMC8759595 | biostudies-literature
UnknownIncV, a FFAT motif-containing Chlamydia protein, tethers the endoplasmic reticulum to the pathogen-containing vacuole.
Not available
S-EPMC5692559 | biostudies-literature
UnknownXopM, An FFAT Motif-Containing Type III Effector Protein From Xanthomonas, Suppresses MTI Responses at the Plant Plasma Membrane.
Not available
S-EPMC11631713 | biostudies-literature
UnknownRDGBα localization and function at membrane contact sites is regulated by FFAT-VAP interactions.
Not available
S-EPMC5818063 | biostudies-literature
UnknownFFAT rescues VAPA-mediated inhibition of ER-to-Golgi transport and VAPB-mediated ER aggregation.
Not available
S-EPMC3038994 | biostudies-literature
ProteomicsIdentification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites
Membrane contact sites are cellular structures that mediate inter-organelle exchange and communication. The endoplasmic reticulum (ER), which forms a network extending throughout the cytoplasm, possesses two known major tether proteins, named VAP-A and VAP-B, that allow its interaction with other or...
ORGANISM(S): Homo sapiens (Human) 
2018-06-05 | PXD009575 | Pride
Endoplasmic reticulum Mospd2 Ffat motif 
UnknownVAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase.
Not available
S-EPMC4068158 | biostudies-literature
UnknownSystematic prediction of FFAT motifs across eukaryote proteomes identifies nucleolar and eisosome proteins with the predicted capacity to form bridges to the endoplasmic reticulum.
Not available
S-EPMC6881177 | biostudies-literature
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