Differences between AGAP1, ASAP1 and Arf GAP1 in substrate recognition: interaction with the N-terminus of Arf1.

摘要: Abstract The Arf GAPs are a structurally diverse group of proteins that catalyze the hydrolysis GTP bound to Arf1. Here, we directly compare role amino acids 2–17 Arf1, GTP- and phospholipid-sensitive switch, for interaction with three GAPs: GAP1, AGAP1 ASAP1. Sequestration an antibody inhibited tested GAPs. Examination Arf1 mutants also indicated [2–17]Arf1 is critical structural determinant all GAPs; however, effect specific mutations differed among Compared wild-type terminal 13 ([Δ13]Arf1) 17 ([Δ17]Arf1) deleted had 200- 4000-fold reduced ASAP1 150-fold AGAP1. In contrast, deletion terminus GAP1 by 5-fold. By analysis point mutants, found lysines 15 16 greater contribution productive between than GAP1. Leucine 8 contributed but not Amino isolated from protein, GAP activity Taken together, our results indicate (i) interact (ii) each subgroup has unique interface