What question did this study set out to answer?

To identify and characterize a novel brain phospholipase D activator distinct from ADP-ribosylation factor and evaluate the structural requirements for its activity.

October 1, 1995Journal of Biological ChemistryOpen Access

Synergistic Activation of Rat Brain Phospholipase D by ADP-ribosylation Factor and rhoA p21, and Its Inhibition by Clostridium botulinum C3 Exoenzyme

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Authors

HKHideo KuribaraUniversity of Tsukuba TKTago KenjiTokyo Institute of Technology TYTakeaki YokozekiTokyo Institute of Technology

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Implication

Biochemical analysis reveals synergistic activation of brain phospholipase D by rhoA p21 and ARF, indicating that lipid modification is critical for dual enzyme regulation.

Key Points

To identify and characterize a novel brain phospholipase D activator distinct from ADP-ribosylation factor and evaluate the structural requirements for its activity.
Purified a cytosolic activating factor from bovine brain using sequential chromatography and identified it via immunoblotting with Rho-family antibodies.
Expressed recombinant isoprenylated rhoA p21 in Sf9 insect cells and non-isoprenylated rhoA p21 in Escherichia coli to measure GTPγS-dependent phospholipase D activation.
Treated native and recombinant rhoA p21 with Clostridium botulinum C3 exoenzyme and NAD to examine how ADP-ribosylation alters enzyme stimulation.
Isoprenylated rhoA p21 stimulated rat brain phospholipase D in a concentration- and GTPγS-dependent manner, whereas non-isoprenylated rhoA p21 failed to activate the enzyme despite identical GTPγS-binding affinity.
Recombinant isoprenylated rhoA p21 and ADP-ribosylation factor acted synergistically to stimulate rat brain phospholipase D activity.
C3 exoenzyme-mediated ADP-ribosylation of rhoA p21 inhibited individual and synergistic phospholipase D activation in direct proportion to the degree of NAD-dependent ribosylation.

Cite This Study

Kuribara et al. (1995) studied this question.

synapsesocial.com/papers/6a8820b1b0d802598bf4da30 https://doi.org/10.1074/jbc.270.43.25667

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Implication

Biochemical analysis reveals synergistic activation of brain phospholipase D by rhoA p21 and ARF, indicating that lipid modification is critical for dual enzyme regulation.

Synergistic Activation of Rat Brain Phospholipase D by ADP-ribosylation Factor and rhoA p21, and Its Inhibition by Clostridium botulinum C3 Exoenzyme

Discussion

Member takes

Implication

Key Points

Cite This Study

Synergistic Activation of Rat Brain Phospholipase D by ADP-ribosylation Factor and rhoA p21, and Its Inhibition by Clostridium botulinum C3 Exoenzyme

Discussion

Member takes

Implication

Key Points

Cite This Study

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