Sort   by:  
 Page size 
UnknownFFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts.
Not available
S-EPMC7705450 | biostudies-literature
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
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 
UnknownFFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts
Not available
S-SCDT-EMBOJ-2019-104369 | biostudies-other
ProteomicsACBD5 phosphorylationsite analysis
Peroxisomes (POs) and the endoplasmic reticulum (ER) cooperate in cellular lipid metabolism and form membrane contacts, which are mediated by the peroxisomal membrane proteins acyl-coenzyme A-binding domain protein 4 and 5 (ACBD4/5) which bind to the resident ER protein vesicle-associated membrane p...
ORGANISM(S): Homo sapiens (Human) 
2022-01-10 | PXD018005 | Pride
Acbd5 Cos7 cells Phosphorylation 
ProteomicsVAPB interacts with phosphorylated ELYS at decondensing chromosomes during mitosis - phosphorylation analysis
ELYS is a nucleoporin that localizes to the nuclear side of the nuclear envelope in interphase cells. In mitosis, it serves as an assembly platform that interacts with chromatin and then with nucleoporin subcomplexes to initiate the formation of novel nuclear pore complexes. Here we describe the int...
ORGANISM(S): Homo sapiens (Human) 
2024-04-17 | PXD048054 | Pride
Elys Ffat-motif Nuclear envelope Vapb Mitosis Ahctf1 
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 
UnknownPhosphoregulation accommodates Type III secretion and assembly of a tether of ER-Chlamydia inclusion membrane contact sites.
Not available
S-EPMC9286742 | biostudies-literature
Sort   by:  
 Page size