N-terminal fatty acylation of the alpha-subunit of the G-protein Gi1: only the myristoylated protein is a substrate for palmitoylation.

Antzeko izenburuak

• Chemical inhibition of myristoylation of the G-protein Gi1 alpha by 2-hydroxymyristate does not interfere with its palmitoylation or membrane association. Evidence that palmitoylation, but not myristoylation, regulates membrane attachment.
  nork: Galbiati, F, et al.
  Argitaratua: (1996)
• A novel N-terminal motif for palmitoylation of G-protein alpha subunits.
  nork: Parenti, M, et al.
  Argitaratua: (1993)
• The palmitoylation status of the G-protein G(o)1 alpha regulates its activity of interaction with the plasma membrane.
  nork: Grassie, M A, et al.
  Argitaratua: (1994)
• The role of palmitoylation of the guanine nucleotide binding protein G11 alpha in defining interaction with the plasma membrane.
  nork: McCallum, J F, et al.
  Argitaratua: (1995)
• Palmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains
  nork: Abrami, Laurence, et al.
  Argitaratua: (2021)