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Related Experiment Videos

Structural analysis of human phospholipase D1

T C Sung1, Y Zhang, A J Morris

  • 1Department of Pharmacological Sciences and the Institute for Cell and Developmental Biology, SUNY at Stony Brook, Stony Brook, New York 11794-8651, USA.

The Journal of Biological Chemistry
|January 28, 1999
PubMed
Summary

Phosphatidylcholine-specific phospholipase D1 (PLD1) activation involves specific amino-terminal regions required for protein kinase C-alpha (PKC-alpha) but not RhoA or ARF1 activation. The PLD1 loop region inhibits activity, while the amino terminus is crucial for regulation.

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Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Enzymology

Background:

  • Phosphatidylcholine-specific phospholipase D (PLD) enzymes are implicated in cellular signal transduction and membrane trafficking.
  • Two mammalian genes, PLD1 and PLD2, encoding PLD activities have been identified.
  • PLD1 activation is known to be synergistically regulated by PKC-alpha, ARF1, and Rho family members.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying PLD1 activation through domain deletion and mutagenesis.
  • To identify specific regions of PLD1 responsible for activation by different signaling molecules.
  • To understand the role of unique PLD1 regions in its enzymatic regulation.

Main Methods:

  • Molecular analysis of PLD1 using domain deletion and site-directed mutagenesis.

Related Experiment Videos

  • In vivo assessment of basal and activated PLD activity.
  • Comparison of PLD1 structure-function relationships with other PLD family members.

    • Main Results:

    • The N-terminal 325 amino acids of PLD1 are essential for PKC-alpha-mediated activation but not for ARF1 or RhoA activation.
    • This N-terminal region also functions to inhibit basal PLD activity in vivo.
    • The PLD1-unique 'loop' region was found to mediate inhibition, not effector regulation, of PLD1 activity.
    • Modifications to the N-terminus are compatible with PLD enzymatic function, while C-terminal modifications are not.

    Conclusions:

    • A model for PLD1 activation is proposed, highlighting the distinct roles of the N-terminus and loop region in regulating enzymatic activity.
    • The N-terminal region is a key regulatory domain, mediating both inhibition of basal activity and facilitating activation by specific signaling pathways.
    • Understanding these regulatory mechanisms provides insight into the complex role of PLD1 in cellular processes.