PMID- 15979509
OWN - NLM
STAT- MEDLINE
DCOM- 20050826
LR  - 20220129
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1744
IP  - 3
DP  - 2005 Jul 10
TI  - The role of the phosphoinositides at the Golgi complex.
PG  - 396-405
AB  - The phosphorylated derivatives of phosphatidylinositol (PtdIns), known as the 
      polyphosphoinositides (PIs), represent key membrane-localized signals in the 
      regulation of fundamental cell processes, such as membrane traffic and 
      cytoskeleton remodelling. The reversible production of the PIs is catalyzed 
      through the combined activities of a number of specific phosphoinositide 
      phosphatases and kinases that can either act separately or in concert on all the 
      possible combinations of the 3, 4, and 5 positions of the inositol ring. So far, 
      seven distinct PI species have been identified in mammalian cells and named 
      according to their site(s) of phosphorylation: PtdIns 3-phosphate (PI3P); PtdIns 
      4-phosphate (PI4P); PtdIns 5-phosphate (PI5P); PtdIns 3,4-bisphosphate (PI3,4P2); 
      PtdIns 4,5-bisphosphate (PI4,5P2); PtdIns 3,5-bisphosphate (PI3,5P2); and PtdIns 
      3,4,5-trisphosphate (PI3,4,5P3). Over the last decade, accumulating evidence has 
      indicated that the different PIs serve not only as intermediates in the synthesis 
      of the higher phosphorylated phosphoinositides, but also as regulators of 
      different protein targets in their own right. These regulatory actions are 
      mediated through the direct binding of their protein targets. In this way, the 
      PIs can control the subcellular localization and activation of their various 
      effectors, and thus execute a variety of cellular responses. To exert these 
      functions, the metabolism of the PIs has to be finely regulated both in time and 
      space, and this is achieved by controlling the subcellular distribution, 
      regulation, and activation states of the enzymes involved in their synthesis and 
      removal (kinases and phosphatases). These exist in many different isoforms, each 
      of which appears to have a distinctive intracellular localization and regulation. 
      As a consequence of this subcompartimentalized PI metabolism, a sort of 
      "PI-fingerprint" of each cell membrane compartment is generated. When combined 
      with the targeted recruitment of their protein effectors and the different 
      intracellular distributions of other lipids and regulatory proteins (such as 
      small GTPases), these factors can maintain and determine the identity of the cell 
      organelles despite the extensive membrane flux []. Here, we provide an overview 
      of the regulation and roles of different phosphoinositide kinases and 
      phosphatases and their lipid products at the Golgi complex.
FAU - De Matteis, Maria Antonietta
AU  - De Matteis MA
AD  - Department of Cell Biology and Oncology, Consorzio Mario Negri Sud, 66030 Santa 
      Maria, Imbaro, Chieti, Italy. dematteis@negrisud.it
FAU - Di Campli, Antonella
AU  - Di Campli A
FAU - Godi, Anna
AU  - Godi A
LA  - eng
GR  - GP0203Y01/TI_/Telethon/Italy
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 (Phosphatidylinositols)
RN  - EC 2.7.1.67 (1-Phosphatidylinositol 4-Kinase)
RN  - EC 3.1.3.- (polyphosphoinositide phosphatase)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
SB  - IM
MH  - 1-Phosphatidylinositol 4-Kinase/*metabolism
MH  - Animals
MH  - Golgi Apparatus/*enzymology
MH  - Phosphatidylinositols/*metabolism
MH  - Phosphoric Monoester Hydrolases/*metabolism
RF  - 74
EDAT- 2005/06/28 09:00
MHDA- 2005/08/27 09:00
CRDT- 2005/06/28 09:00
PHST- 2005/02/21 00:00 [received]
PHST- 2005/04/28 00:00 [revised]
PHST- 2005/04/28 00:00 [accepted]
PHST- 2005/06/28 09:00 [pubmed]
PHST- 2005/08/27 09:00 [medline]
PHST- 2005/06/28 09:00 [entrez]
AID - S0167-4889(05)00081-9 [pii]
AID - 10.1016/j.bbamcr.2005.04.013 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2005 Jul 10;1744(3):396-405. doi: 
      10.1016/j.bbamcr.2005.04.013.