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Reconstitution of GTP‐γ‐S‐dependent phospholipase D activity with ARF, RhoA, and a soluble 36‐kDa protein
Author(s) -
Shimooku Kiyoshi,
Akisue Toshihiro,
Jinnai Hitoshi,
Hitomi Tomohiro,
Ogino Chiaki,
Yoshida Kimihisa,
Nakamura Shun-ichi,
Nishizuka Yasutomi
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00483-8
Subject(s) - rhoa , cytosol , gtp' , phospholipase d , adp ribosylation factor , g protein , phospholipase , phospholipase c , gtpase , chemistry , gtpase activating protein , biochemistry , microbiology and biotechnology , enzyme , biology , signal transduction , cell , golgi apparatus
For activation of kidney membrane phospholipase D (PLD), cytosol is absolutely needed in addition to GTP‐γ‐S. The active component of cytosol consists of three protein factors: ADP‐ribosylation factor, RhoA, and a soluble 36‐kDa protein. Any combination of these two factors synergistically activates PLD to some extent, but the presence of the three factors causes full activation. The 36‐kDa protein is stable at 60°C but inactivated at 80°C for 10 min. Tissue distribution of the 36‐kDa protein roughly coincides with that of PLD, suggesting physiological relevance of the protein in the regulation of PLD.