The inhibition of the GTPase activating protein-Ha-ras interaction by acidic lipids is due to physical association of the C-terminal domain of the GTPase activating protein with micellar structures.

Documenti analoghi

• Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity.
  di: Gideon, P, et al.
  Pubblicazione: (1992)
• Ha-ras proteins exhibit GTPase activity: point mutations that activate Ha-ras gene products result in decreased GTPase activity.
  di: Manne, V, et al.
  Pubblicazione: (1985)
• Ras GTPase activating (RasGAP) activity of the dual specificity GAP protein Rasal requires colocalization and C2 domain binding to lipid membranes
  di: Sot, Begoña, et al.
  Pubblicazione: (2013)
• GTPase activity of Di-Ras proteins is stimulated by Rap1GAP proteins
  di: Gasper, Raphael, et al.
  Pubblicazione: (2010)
• A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-activating protein
  di: Kötting, Carsten, et al.
  Pubblicazione: (2006)