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Mammalian phospholipase D structure and regulation.
M A Frohman1, T C Sung, A J Morris
1Department of Pharmacological Sciences, Institute for Cell and Developmental Biology, SUNY at Stony Brook, Stony Brook, NY 1794-8651, USA. michael@pharm.som.sunysb.edu
Biochimica Et Biophysica Acta
|July 30, 1999
Summary
New studies on phospholipase D1 and 2 (PLD) reveal their structure and regulation. PLD enzymes are crucial for cellular processes like secretion and membrane biogenesis.
Area of Science:
- Biochemistry
- Cell Biology
Background:
- Phospholipase D (PLD) enzymes play critical roles in cellular signaling and membrane trafficking.
- The recent cloning of cDNA for phospholipase D1 and 2 (PLD1 and PLD2) enables detailed investigation into their molecular characteristics.
Purpose of the Study:
- To explore the structure and regulation of phospholipase D1 and 2.
- To understand the enzymatic mechanisms and in vivo functions of PLD enzymes.
Main Methods:
- Identification and characterization of cDNA clones for PLD1 and PLD2.
- Analysis of catalytic domains and comparison to phosphodiesterases.
- Investigation of in vivo roles in cellular processes.
Main Results:
- PLD activity is encoded by at least two genes, PLD1 and PLD2.
- These genes possess catalytic domains suggesting a mechanism related to phosphodiesterases.
- In vivo studies indicate PLD involvement in secretion, endocytosis, and membrane biogenesis.
Conclusions:
- Phospholipase D1 and 2 are key enzymes with conserved catalytic domains.
- PLD enzymes are essential for fundamental cellular functions including membrane dynamics and transport.