PMID- 10425403
OWN - NLM
STAT- MEDLINE
DCOM- 19990909
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1439
IP  - 2
DP  - 1999 Jul 30
TI  - Structural organization of mammalian lipid phosphate phosphatases: implications
      for signal transduction.
PG  - 299-316
AB  - This article describes the regulation of cell signaling by lipid phosphate
      phosphatases (LPPs) that control the conversion of bioactive lipid phosphates to 
      their dephosphorylated counterparts. A structural model of the LPPs, that were
      previously called Type 2 phosphatidate phosphatases, is described. LPPs are
      characterized by having no Mg(2+) requirement and their insensitivity to
      inhibition by N-ethylmaleimide. The LPPs have six putative transmembrane domains 
      and three highly conserved domains that define a phosphatase superfamily. The
      conserved domains are juxtaposed to the proposed membrane spanning domains such
      that they probably form the active sites of the phosphatases. It is predicted
      that the active sites of the LPPs are exposed at the cell surface or on the
      luminal surface of intracellular organelles, such as Golgi or the endoplasmic
      reticulum, depending where various LPPs are expressed. LPPs could attenuate cell 
      activation by dephosphorylating bioactive lipid phosphate esters such as
      phosphatidate, lysophosphatidate, sphingosine 1-phosphate and ceramide
      1-phosphate. In so doing, the LPPs could generate alternative signals from
      diacylglycerol, sphingosine and ceramide. The LPPs might help to modulate cell
      signaling by the phospholipase D pathway. For example, phosphatidate generated
      within the cell by phospholipase D could be converted by an LPP to
      diacylglycerol. This should change the relative balance of signaling by these two
      lipids. Another possible function of the LPPs relates to the secretion of
      lysophosphatidate and sphingosine 1-phosphate by activated platelets and other
      cells. These exogenous lipids activate phospholipid growth factor receptors on
      the surface of cells. LPP activities could attenuate cell activation by
      lysophosphatidate and sphingosine 1-phosphate through their respective receptors.
FAU - Waggoner, D W
AU  - Waggoner DW
AD  - Department of Biochemistry (Signal Transduction Laboratories), Lipid and
      Lipoprotein Research Group, University of Alberta, 357 Heritage Medical Research 
      Centre, Edmonton, Alberta T6G 2S2, Canada.
FAU - Xu, J
AU  - Xu J
FAU - Singh, I
AU  - Singh I
FAU - Jasinska, R
AU  - Jasinska R
FAU - Zhang, Q X
AU  - Zhang QX
FAU - Brindley, D N
AU  - Brindley DN
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Ceramides)
RN  - 0 (Diglycerides)
RN  - 0 (Sphingolipids)
RN  - EC 3.1.3.4 (Phosphatidate Phosphatase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bacteria
MH  - Ceramides/metabolism
MH  - *Conserved Sequence
MH  - Diglycerides/metabolism
MH  - Gene Expression Regulation, Enzymologic
MH  - Humans
MH  - Molecular Sequence Data
MH  - Phosphatidate Phosphatase/chemistry/genetics/*metabolism
MH  - Phosphorylation
MH  - Sequence Alignment
MH  - *Signal Transduction
MH  - Sphingolipids/metabolism
MH  - Substrate Specificity
MH  - Terminology as Topic
MH  - Yeasts
RF  - 106
EDAT- 1999/07/30 00:00
MHDA- 1999/07/30 00:01
CRDT- 1999/07/30 00:00
PHST- 1999/07/30 00:00 [pubmed]
PHST- 1999/07/30 00:01 [medline]
PHST- 1999/07/30 00:00 [entrez]
AID - S1388-1981(99)00102-X [pii]
AID - 10.1016/s1388-1981(99)00102-x [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Jul 30;1439(2):299-316. doi:
      10.1016/s1388-1981(99)00102-x.