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The potential role for Cdc42 protein from rat brain cytosol in phospholipase D activation
Author(s) -
Han JoongSoo,
Kim HyungChul,
Chung JoonKi,
Kang HeunSoo,
Donaldson Jason,
Koh JaiKyung
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800203312
Subject(s) - cytosol , cdc42 , microbiology and biotechnology , chemistry , phospholipase , phospholipase d , phospholipase a , biochemistry , phospholipase a2 , biology , enzyme , signal transduction
Phospholipase D (PLD) has been extracted from rat brain membranes and chromatographically enriched 70‐fold. From the rat brain cytosol, Cdc42 with a Mr of about 24,000 and ADP‐ribosylation Factor (Arf) with a Mr of about 18,000 have been purified to near homogeneity. PLD was activated better by purified cytosolic Arf than by the other small G proteins tested. Cdc42 purified from rat brain cytosol showed 70% of PLD activation activity exerted by cytosolic Arf, suggesting that Cdc42 may be one of the major G proteins involved in the activation of membrane‐associated PLD. While Cdc42 or RhoA exhibited synergistic activation of PLD when administered in conjunction with Arf, Cdc42 and RhoA showed an additive effect when used together. It is possible that Arf and Rho family proteins may have different interaction sites on PLD. These findings support a role for GTP‐binding proteins of the Rho family as well as Arf in the activation of membrane‐associated PLD and further suggest that Cdc42 may be a major G protein involved in the PLD activation in rat brain.