text: Results
  The observation that AP-3 is found in both cytosolic and membrane subcellular fractions, and that membrane-associated AP-3 can be extracted with salts (Dell'Angelica et al., 1997a) is consistent with its role as a membrane coat that can be recruited from a cytosolic pool. In addition, the punctate staining of AP-3 by immunofluorescence microscopy, its redistribution to the cytosol by BFA, and the reversibility of the BFA effect (Dell'Angelica et al., 1997a; Simpson et al., 1997) also indicate that AP-3 can cycle between the cytosol and membranes. The sensitivity of AP-3 to BFA in cells suggests that its membrane association may be regulated by ARF1, since BFA inhibits ARF1 guanine nucleotide exchange, and has been shown to prevent ARF1 membrane binding in vitro (Donaldson et al., 1992; Helms and Rothman, 1992; Randazzo et al., 1993).
  
  
entities.text: ['cytosolic']
entities.type: Organism_substance
entities.entity_id: PMC-2133064-sec-12_T1
entities.text: ['membrane subcellular fractions']
entities.type: Organism_substance
entities.entity_id: PMC-2133064-sec-12_T2
entities.text: ['membrane']
entities.type: Cellular_component
entities.entity_id: PMC-2133064-sec-12_T3
entities.text: ['membrane']
entities.type: Cellular_component
entities.entity_id: PMC-2133064-sec-12_T4
entities.text: ['cytosolic pool']
entities.type: Organism_substance
entities.entity_id: PMC-2133064-sec-12_T5
entities.text: ['cytosol']
entities.type: Organism_substance
entities.entity_id: PMC-2133064-sec-12_T6
entities.text: ['cytosol']
entities.type: Organism_substance
entities.entity_id: PMC-2133064-sec-12_T7
entities.text: ['membranes']
entities.type: Cellular_component
entities.entity_id: PMC-2133064-sec-12_T8
entities.text: ['cells']
entities.type: Cell
entities.entity_id: PMC-2133064-sec-12_T9
entities.text: ['membrane']
entities.type: Cellular_component
entities.entity_id: PMC-2133064-sec-12_T10
entities.text: ['membrane']
entities.type: Cellular_component
entities.entity_id: PMC-2133064-sec-12_T11