p23rab2, a ras-like GTPase with a -GGGCC C-terminus, is isoprenylated but not detectably carboxymethylated in NIH3T3 cells.

Abstract:

:With the development of a specific anti-rab2 antiserum, p23rab2, a ras-like GTPase with a -GGGCC C-terminus, has been localized mainly to the particulate (P100) fraction in NIH3T3 cells, although a small amount of this protein also appears in the soluble fraction. The endogenous p23rab2 is isoprenylated in intact cells, and recombinant murine p23rab2 is also isoprenylated in an in vitro system using reticulocyte lysate. Both the cytosolic and membrane-bound forms of p23rab2 are isoprenylated in intact cells. Recombinant p23rab2 is specifically geranylgeranylated at one or both of the C-terminal cysteine residues in the in vitro system. Blocking isoprenoid synthesis with lovastatin results in an accumulation of a totally cytosolic unisoprenylated form, indicating that isoprenylation is a prerequisite for membrane association of p23rab2. Surprisingly, unlike p21ras and p25rab3A, no carboxymethylation of p23rab2 is detectable in either the soluble or particulate fractions.

journal_name

Oncogene

journal_title

Oncogene

authors

Wei C,Lutz R,Sinensky M,Macara IG

subject

Has Abstract

pub_date

1992-03-01 00:00:00

pages

467-73

issue

3

eissn

0950-9232

issn

1476-5594

journal_volume

7

pub_type

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