1. AlFx affects the formation of focal complexes by stabilizing the Arf-GAP ASAP1 in a complex with Arf1
- Author
-
Frédéric Luton, Stéphanie Klein, Michel Franco, Pierre Chardin, Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (... - 2019) (UNS), and COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
RHOA ,GTPase-activating protein ,ADP ribosylation factor ,Biophysics ,CDC42 ,Transfection ,Biochemistry ,03 medical and health sciences ,Fluorides ,Structural Biology ,In vivo ,Cricetinae ,Genetics ,Homologous chromosome ,Animals ,Aluminum Compounds ,Molecular Biology ,Paxillin ,Cells, Cultured ,030304 developmental biology ,Adaptor Proteins, Signal Transducing ,0303 health sciences ,Aluminum fluoride ,biology ,ADP-Ribosylation Factors ,Focal complex ,030302 biochemistry & molecular biology ,GTPase-Activating Proteins ,food and beverages ,Cell Biology ,In vitro ,3. Good health ,Cell biology ,ASAP1 ,ADP-ribosylation factor ,biology.protein ,ADP-Ribosylation Factor 1 - Abstract
Aluminum fluoride (AlFx) is known to activate directly the α subunit of G-proteins but not the homologous small GTP-binding proteins. However, AlFx can stabilize complexes formed between Ras, RhoA or Cdc42 and their corresponding GTPase-activating proteins (GAPs). Here, we demonstrate that Arf1GDP can be converted into an active conformation by AlFx to form a complex with the Arf-GAP ASAP1 in vitro and in vivo. Within this complex ASAP1, which GAP activity is inoperative, can still alter the recruitment of paxillin to the focal complexes, thus indicating that ASAP1 interferes with focal complexes independently of its GAP activity.
- Published
- 2005