id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-298251-u36lb44w	Donaldson, Julie G.	Arf Family G Proteins and their regulators: roles in membrane transport, development and disease	2011-05-18		.txt	text/plain	10702	519	44	Members of the ADP-ribosylation factor (ARF) family of guanine-nucleotide-binding (G) proteins, including the ARF-like (ARL) proteins and SAR1, regulate membrane traffic and organelle structure by recruiting cargo-sorting coat proteins, modulating membrane lipid composition, and interacting with regulators of other G proteins. ARF proteins at the trans-Golgi network (TGN) also recruit heterotetrameric clathrin adaptor protein 1 (AP1), AP3 and AP4, as well as the three monomeric Golgi-localized, γ-ear-containing, ADP-ribosylation factor-binding Figure 1 | The domain structure and regulation of ARF and ARLs. a | A schematic of representative ADP-ribosylation factor (ARF), SAR1 and ARF-like (ARL) proteins, indicating the conserved amino-terminal amphipathic helix and the protein-specific lipid modifications at the N terminus. ARF6 at the plasma membrane can regulate the membrane lipid composition, alterations in cortical actin to drive protrusions (for example, during cell migration), and endocytosis of ligand-activated guanine-nucleotide-binding (G) protein-coupled receptors (GPCR) via clathrin-dependent endocytosis.	./cache/cord-298251-u36lb44w.txt	./txt/cord-298251-u36lb44w.txt