Abstract
Many G protein α subunits are dually acylated with myristate and palmitate or are palmitoylated on more than one cysteine residue near their N termini. The Gα protein that activates adenylyl cyclase, αs, is not myristoylated but can be reversibly palmitoylated. It appears that αs contains another, as-yet-unidentified covalent modification that decreases its apparent dissociation constant for adenylyl cyclase from 50 nM to <0.5 nM. This modification is at or near the N terminus of the protein and is hydrophobic. Palmitoylation of native αs does not account for its high affinity for adenylyl cyclase.
Original language | English (US) |
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Pages (from-to) | 6116-6120 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 94 |
Issue number | 12 |
DOIs | |
State | Published - Jun 10 1997 |
ASJC Scopus subject areas
- General