Journal of Advanced Research, 2023 Introduction: Acquired resistance to BRAF inhibitor vemurafenib is frequently observed in metastatic colorectal cancer (CRC), and it is a thorny issue that results in treatment failure.
Qing-Yu He, Hui-Fang Hu
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Structural basis for activation of Arf1 at the Golgi complex
Cell Reports, 2022 Summary The Golgi complex is the central sorting station of the eukaryotic secretory pathway. Traffic through the Golgi requires activation of Arf GTPases that orchestrate cargo sorting and vesicle formation by recruiting an array of effector proteins.
J Christopher Fromme
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ARF1 and SAR1 GTPases in Endomembrane Trafficking in Plants [PDF]
International Journal of Molecular Sciences, 2013 Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their functional and sequential characteristics.
Birsen Cevher Keskin
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Structural basis for the dynamic conformations of AP-4 and its association with ARF1 [PDF]
Nature CommunicationsAmong the distinct adaptor protein (AP) complexes, AP-4 primarily functions as a non-clathrin-coated vesicle machinery essential for intracellular membrane trafficking. ARF1 is a master regulator of AP-4 membrane recruitment, but the underlying mechanism
Yanghui Wang +6 more
doaj +2 more sources
Arf GTPases Define BST-2-Independent Pathways for HIV-1 Assembly and Release [PDF]
VirusesADP-ribosylation factor (Arf) proteins are small GTPases that regulate intracellular membrane trafficking and actin remodeling through tightly controlled cycles of GTP binding and hydrolysis.
Adam Smith +4 more
doaj +2 more sources
ARF1 recruits RAC1 to leading edge in neutrophil chemotaxis [PDF]
Cell Communication and Signaling, 2017 Background The small GTPase ARF1 mediates membrane trafficking mostly from the Golgi, and is essential for the G protein-coupled receptor (GPCR)-mediated chemotaxis of neutrophils.
Yuichi Mazaki +5 more
doaj +4 more sources
Arf1 and membrane curvature cooperate to recruit Arfaptin2 to liposomes. [PDF]
PLoS ONE, 2013 Arfaptin2 contains a Bin/Amphiphysin/Rvs (BAR) domain and directly interacts with proteins of the Arf/Arl family in their active GTP-bound state. It has been proposed that BAR domains are able to sense membrane curvature and to induce membrane tubulation.
Ernesto E Ambroggio +4 more
doaj +4 more sources
In vivo monitoring of the recruitment and activation of AP-1 by Arf1 [PDF]
Scientific Reports, 2017 AP-1 is a clathrin adaptor recruited to the trans-Golgi Network where it can interact with specific signals found in the cytosolic tail of cargo proteins to incorporate them into clathrin-coated vesicles for trafficking.
Etienne Sauvageau +2 more
doaj +5 more sources
Arf1 GTPase Regulates Golgi‐Dependent G2/M Transition and Spindle Organization in Oocyte Meiosis
Advanced ScienceADP‐ribosylation factor 1 (Arf1) is a small GTPase belonging to the Arf family. As a molecular switch, Arf1 is found to regulate retrograde and intra‐Golgi transport, plasma membrane signaling, and organelle function during mitosis.
Shao-Chen Sun
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AMPK regulates ARF1 localization to membrane contact sites to facilitate fatty acid transfer between lipid droplets and mitochondria [PDF]
Cell Death and DiseaseLipid droplet (LD) -mitochondrion contacts play a crucial role in regulating energy metabolism and fatty acid oxidation in skeletal muscle cells. However, the proteins that regulate these interactions remain poorly understood.
Lupeng Chen +5 more
doaj +2 more sources