Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Phospholipase D.

J H Exton1

  • 1Howard Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0295, USA. john.exton@mcmail.vanderbilt.edu

Annals of the New York Academy of Sciences
|May 20, 2000
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Phospholipase D-structure, regulation and function.

Reviews of physiology, biochemistry and pharmacology·2002
Same author

Arfophilin is a common target of both class II and class III ADP-ribosylation factors.

Biochemistry·2001
Same author

Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1.

Biochemical and biophysical research communications·2001
Same author

Phospholipase D activity is required for actin stress fiber formation in fibroblasts.

Molecular and cellular biology·2001
Same author

Determination of interaction sites of phospholipase D1 for RhoA.

The Biochemical journal·2001
Same author

Requirements and effects of palmitoylation of rat PLD1.

The Journal of biological chemistry·2000

Phospholipase D (PLD) enzymes hydrolyze phosphatidylcholine, impacting cell growth and secretion. Mammalian PLD1 and PLD2 isoforms have distinct regulatory pathways, but their specific functions and locations require further investigation.

Area of Science:

  • Biochemistry
  • Cell Biology

Background:

  • Phospholipase D (PLD) is a ubiquitous enzyme catalyzing the hydrolysis of phosphatidylcholine into phosphatidic acid and choline.
  • The produced phosphatidic acid plays a role in cellular processes such as cell growth, shape modulation, and secretion.
  • Two mammalian genes encode PLD, resulting in alternatively spliced PLD1 and PLD2 isoforms.

Purpose of the Study:

  • To elucidate the distinct characteristics and functions of the two mammalian phospholipase D isoforms, PLD1 and PLD2.
  • To investigate the regulatory mechanisms governing PLD1 and PLD2 activity.

Main Methods:

  • Analysis of conserved catalytic domains (HKD motifs) essential for enzyme activity and dimerization.
  • Investigation of regulatory interactions with protein kinase C and small GTPases (Rho and ARF families).

Related Experiment Videos

Main Results:

  • Both PLD1 and PLD2 possess two conserved HKD motifs crucial for catalysis and dimerization.
  • PLD1 demonstrates regulation by protein kinase C and Rho/ARF GTPases.
  • PLD2 exhibits higher basal activity and is less responsive to these regulatory proteins.

Conclusions:

  • Mammalian PLD1 and PLD2 are distinct isoforms with differential regulation.
  • The precise cellular localization and specific biological functions of PLD1 and PLD2 warrant further research.