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.

Eitemau Tebyg

• N-terminal fatty acylation of the alpha-subunit of the G-protein Gi1: only the myristoylated protein is a substrate for palmitoylation.
  gan: Galbiati, F, et al.
  Cyhoeddwyd: (1994)
• The palmitoylation status of the G-protein G(o)1 alpha regulates its activity of interaction with the plasma membrane.
  gan: Grassie, M A, et al.
  Cyhoeddwyd: (1994)
• The role of palmitoylation of the guanine nucleotide binding protein G11 alpha in defining interaction with the plasma membrane.
  gan: McCallum, J F, et al.
  Cyhoeddwyd: (1995)
• Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae.
  gan: Robbins, S M, et al.
  Cyhoeddwyd: (1995)
• Myristoylation of an inhibitory GTP-binding protein alpha subunit is essential for its membrane attachment.
  gan: Jones, T L, et al.
  Cyhoeddwyd: (1990)