Lipid phosphate phosphatases (LPP1–LPP3) have been topographically modelled as monomers (molecular mass of 31–36 kDa) composed of six transmembrane domains and with the catalytic site facing the extracellular side of the plasma membrane or the luminal side of intracellular membranes. The catalytic motif has three conserved domains, termed C1, C2 and C3. The C1 domain may be involved in substrate recognition, whereas C2 and C3 domains appear to participate in the catalytic dephosphorylation of the substrate. We have obtained three lines of evidence to demonstrate that LPPs exist as functional oligomers. First, we have used recombinant expression and immunoprecipitation analysis to demonstrate that LPP1, LPP2 and LPP3 form both homo- and hetero-oligomers. Secondly, large LPP oligomeric complexes that are catalytically active were isolated using gel-exclusion chromatography. Thirdly, we demonstrate that catalytically deficient guinea-pig FLAG-tagged H223L LPP1 mutant can form an oligomer with wild-type LPP1 and that wild-type LPP1 activity is preserved in the oligomer. These findings suggest that, in an oligomeric arrangement, the catalytic site of the wild-type LPP can function independently of the catalytic site of the mutant LPP. Finally, we demonstrate that endogenous LPP2 and LPP3 form homo- and hetero-oligomers, which differ in their subcellular localization and which may confer differing spatial regulation of phosphatidic acid and sphingosine 1-phosphate signalling.
Skip Nav Destination
Article navigation
April 2008
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkEditorial Board
Research Article|
March 27 2008
Lipid phosphate phosphatases form homo- and hetero-oligomers: catalytic competency, subcellular distribution and function
Jaclyn S. Long;
Jaclyn S. Long
1Cell Biology Group, Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, 27 Taylor Street, Glasgow G4 0NR, Scotland, U.K.
Search for other works by this author on:
Nigel J. Pyne;
Nigel J. Pyne
1Cell Biology Group, Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, 27 Taylor Street, Glasgow G4 0NR, Scotland, U.K.
Search for other works by this author on:
Susan Pyne
Susan Pyne
1
1Cell Biology Group, Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, 27 Taylor Street, Glasgow G4 0NR, Scotland, U.K.
1To whom correspondence should be addressed (email susan.pyne@strath.ac.uk).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
November 27 2007
Revision Received:
December 19 2007
Accepted:
January 08 2008
Accepted Manuscript online:
January 08 2008
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem J (2008) 411 (2): 371–377.
Article history
Received:
November 27 2007
Revision Received:
December 19 2007
Accepted:
January 08 2008
Accepted Manuscript online:
January 08 2008
Citation
Jaclyn S. Long, Nigel J. Pyne, Susan Pyne; Lipid phosphate phosphatases form homo- and hetero-oligomers: catalytic competency, subcellular distribution and function. Biochem J 15 April 2008; 411 (2): 371–377. doi: https://doi.org/10.1042/BJ20071607
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.