Abstract
The recent identification of cDNA clones for phospholipase D has opened the door to new types of investigations into its structure and regulation. PLD activity has been found to be encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may be important for multiples steps in regulated secretion and membrane biogenesis. Copyright (C) 1999 Elsevier Science Ireland Ltd.
| Original language | English |
|---|---|
| Pages (from-to) | 127-140 |
| Number of pages | 14 |
| Journal | Chemistry and Physics of Lipids |
| Volume | 98 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - Apr 1999 |
Bibliographical note
Funding Information:The authors thank laboratory members for critical reading of the manuscript. This work was supported by grants from the NIH to AIM (GM50388) and MAF (GM54813).
Funding
The authors thank laboratory members for critical reading of the manuscript. This work was supported by grants from the NIH to AIM (GM50388) and MAF (GM54813).
| Funders | Funder number |
|---|---|
| National Institutes of Health (NIH) | GM54813 |
| National Institute of General Medical Sciences | R01GM050388 |
Keywords
- ARF
- PLD1
- PLD2
- Phospholipase D
- Protein kinase C
- Rho
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Organic Chemistry
- Cell Biology
Fingerprint
Dive into the research topics of 'Phospholipase D structure and regulation'. Together they form a unique fingerprint.Cite this
- APA
- Author
- BIBTEX
- Harvard
- Standard
- RIS
- Vancouver