A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane

JF Hancock, H Paterson, CJ Marshall - Cell, 1990 - cell.com
JF Hancock, H Paterson, CJ Marshall
Cell, 1990cell.com
The C-terminal CAAX motif of fas proteins undergoes a triplet of posttranslational
modifications that are required for membrane association. The CAAX motif lies immediately
C-terminal to the hypervariable domain, a region of 20 amino acids that distinguishes the ras
proteins from each other. The hypervarlable domains of p21 ur, p21 un*, and p21K-'**(*)
contain she8 for palmltoylation, which we now show must combine with the CAAX motif to
target specific plasma membrane localization. Wlthln the hypervariable domain of~ 21 …
Summary
The C-terminal CAAX motif of fas proteins undergoes a triplet of posttranslational modifications that are required for membrane association. The CAAX motif lies immediately C-terminal to the hypervariable domain, a region of 20 amino acids that distinguishes the ras proteins from each other. The hypervarlable domains of p21 ur, p21 un*, and p21K-‘**(*) contain she8 for palmltoylation, which we now show must combine with the CAAX motif to target specific plasma membrane localization. Wlthln the hypervariable domain of~ 21~-~**@), which Is not palmitoylated, we have identified a navel plasma membrane targeting slgnal consist-Ing of a polybaslc domain that also acts in comblnstion with the CAAX motif. One function of the hypervariable domains of~ 21” s is therefore to provide different signals for plasma membrane localization.
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