{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nVAPA is an integral endoplasmic reticulum protein that functions as a dynamic tether at multiple membrane contact sites, thereby regulating inter‐organelle lipid exchange and membrane trafficking. It achieves this by binding to a range of FFAT (two phenylalanines in an acidic tract) motif–containing proteins, such as the glycolipid transfer protein (GLTP) (PMID 19665998 [4]) and the oxysterol‐binding protein (OSBP) (PMID 20178991 [5]), to coordinate the nonvesicular transport of bioactive lipids like ceramide and cholesterol between the ER and the Golgi. VAPA also partners with ceramide transfer protein (CERT) (PMID 24569996 [10]) and the oxysterol‐binding protein–related protein ORP3 (PMID 25447204 [11]) to regulate lipid flux, while its interactions with factors such as the CARTS (carriers of the trans‐Golgi network to the cell surface)–associated machinery (PMID 26490117 [12]) and the endosomal tethering system (PMID 27419871 [13]) highlight its central role in maintaining lipid homeostasis. Further, by binding ACBD5 to tether peroxisomes (PMID 28108526 [14]) and interacting with novel ER‐anchored tethers like MOSPD2 (PMID 29858488 [16]), VAPA contributes to a diverse network of inter‐organelle communication. Its inherent flexibility, conferred by intrinsically disordered regions, enables it to adapt to varying membrane contacts (PMID 30018135 [17], PMID 36693319 [23])."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of viral infections and neuronal signaling, VAPA (and its homologues) serves as an essential adaptor that bridges viral and host proteins as well as modulates cytoskeletal dynamics. For example, in hepatitis C virus (HCV) infection the VAPA homologue hVAP‐33 critically nucleates the viral RNA replication complex by mediating interactions among HCV nonstructural proteins (PMID 15016871 [1]), an effect further influenced by antiviral proteins such as viperin (PMID 21957124 [7]) and by the bridging factor GPS2 that enhances NS5A–VAPA association (PMID 24223774 [9]). Similar strategies of hijacking VAPA are employed by Aichi virus to assemble cholesterol‐rich replication organelles (PMID 29367253 [15]), while in neuronal cells VAPA interacts with protrudin through a FFAT motif to promote neurite outgrowth and proper subcellular distribution (PMID 19289470 [3]). Detailed structural studies have elucidated the molecular determinants of these FFAT‐dependent interactions, underscoring VAPA's central role in coordinating diverse protein complexes (PMID 34312846 [22]). Moreover, VAPA contributes to the formation of a tripartite complex (VOR complex) with ORP3 and Rab7 that facilitates the nuclear transfer of extracellular vesicle cargo (PMID 30741620 [18])."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAlterations in VAPA expression and function are increasingly implicated in human disease, including cancer and neurodegeneration. Comparative studies of VAP isoforms have revealed that differences in conserved motifs render VAPA resistant to deleterious mutations that affect its homolog VAPB, which is linked to motor neuron disease (PMID 18713837 [2], PMID 21144830 [6]). In oncology, a circular RNA derived from the VAPA locus (circVAPA) is significantly upregulated in colorectal cancer and acts as an oncogenic microRNA sponge to promote tumor progression (PMID 30797148 [19]). Similarly, exosomal long noncoding RNAs such as LINC01833 can modulate VAPA activity to enhance non–small cell lung cancer malignancy and foster an immunosuppressive microenvironment via M2 macrophage polarization (PMID 39152098 [25]). In addition, VAPA contributes to protein sorting into extracellular vesicles, influencing intercellular communication in the tumor microenvironment (PMID 37926697 [24]), and it is involved in ER quality control through interactions with the soluble ER‐phagy receptor CALCOCO1 (PMID 32525583 [20]). Notably, while VAPA is critical for many cellular processes, studies in herpesvirus infection indicate that its function can be context dependent, as its depletion had minimal impact on nuclear egress of these viruses (PMID 34200728 [21])."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jessica Tuuf, Lina Wistbacka, Peter Mattjus "}, {"type": "b", "children": [{"type": "t", "text": "The glycolipid transfer protein interacts with the vesicle-associated membrane protein-associated protein VAP-A."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2009.08.023"}], "href": "https://doi.org/10.1016/j.bbrc.2009.08.023"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19665998"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19665998"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Kyoko Furuita, JunGoo Jee, Harumi Fukada, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109.082602"}], "href": "https://doi.org/10.1074/jbc.M109.082602"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20178991"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20178991"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Keigo Kumagai, Miyuki Kawano-Kawada, Kentaro Hanada "}, {"type": "b", "children": [{"type": "t", "text": "Phosphoregulation of the ceramide transport protein CERT at serine 315 in the interaction with VAMP-associated protein (VAP) for inter-organelle trafficking of ceramide in mammalian cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M113.528380"}], "href": "https://doi.org/10.1074/jbc.M113.528380"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24569996"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24569996"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Marion Weber-Boyvat, Henriikka Kentala, Johanna Lilja, et al. 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