同: PtdIns(3,4)P2, PIP2

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/05/27 22:17:20」(JST)

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Chemical structure of sn-1-stearoyl-2-arachidonoyl phosphatidylinositol (3,4)-bisphosphate

Phosphatidylinositol (3,4)-bisphosphate (PtdIns(3,4)P₂) is a minor phospholipid component of cell membranes, yet an important second messenger. The generation of PtdIns(3,4)P₂ at the plasma membrane activates a number of important cell signaling pathways.^[1]

PtdIns(3,4)P₂ is dephophosphorylated by the phosphatase INPP4B on the 4 position of the inositol ring and by the TPTE (transmembrane phosphatases with tensin homology) family of phosphatases on the 3 position of the inositol ring.

The PH domain in a number of proteins binds to PtdIns(3,4)P₂ including the PH domain in PKB. The generation of PtdIns(3,4)P₂ at the plasma membrane upon the activation of class I PI 3-kinases and SHIP phosphatases causes these proteins to translocate to the plasma membrane, thereby affecting their activity.

References

^ Dimitrios Karathanassis, Robert V. Stahelin, Jerónimo Bravo, Olga Perisic, Christine M Pacold, Wonhwa Cho and Roger L Williams (2002). "Binding of the PX domain of p47phox to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction". EMBO Journal 21 (19): 5057–5068. doi:10.1093/emboj/cdf519. PMC 129041. PMID 12356722.

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English Journal

Phosphoinositide 5- and 3-phosphatase activities of a voltage-sensing phosphatase in living cells show identical voltage dependence.

Keum D1, Kruse M2, Kim DI1, Hille B3, Suh BC3.
Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2016 Jun 28;113(26):E3686-95. doi: 10.1073/pnas.1606472113. Epub 2016 May 24.
Voltage-sensing phosphatases (VSPs) are homologs of phosphatase and tensin homolog (PTEN), a phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2] and phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] 3-phosphatase. However, VSPs have a wider range of substrates, cleaving 3-phosphate from PI(3,4)P2
PMID 27222577

Phosphatidylinositol-3-phosphate is light-regulated and essential for survival in retinal rods.

He F1, Agosto MA1, Anastassov IA1, Tse DY2,3, Wu SM2, Wensel TG1,2.
Scientific reports.Sci Rep.2016 Jun 1;6:26978. doi: 10.1038/srep26978.
Phosphoinositides play important roles in numerous intracellular membrane pathways. Little is known about the regulation or function of these lipids in rod photoreceptor cells, which have highly active membrane dynamics. Using new assays with femtomole sensitivity, we determined that whereas levels
PMID 27245220

Lipid regulators of Pkh2 in Candida albicans, the protein kinase ortholog of mammalian PDK1.

Pastor-Flores D1, Schulze JO1, Bahí A2, Süß E1, Casamayor A3, Biondi RM4.
Biochimica et biophysica acta.Biochim Biophys Acta.2016 Mar;1861(3):249-59. doi: 10.1016/j.bbalip.2015.12.016. Epub 2015 Dec 29.
Pkh is the yeast ortholog of the mammalian 3-phosphoinositide-dependent protein kinase 1 (PDK1). Pkh phosphorylates the activation loop of Ypks, Tpks, Sch9 and also phosphorylates the eisosome components Lsp1 and Pil1, which play fundamental roles upstream of diverse signaling pathways, including th
PMID 26743850

Japanese Journal

The Importance of Interaction with Membrane Lipids through the Pleckstrin Homology Domain of the Guanine Nucleotide Exchange Factor for Rho Family Small Guanosine Triphosphatase, FLJ00018

Biological and Pharmaceutical Bulletin 36(7), 1204-1207, 2013
NAID 130003361463

Parotid Secretory Protein Binds Phosphatidylinositol (3,4) Bisphosphate

Journal of dental research 90(9), 1085-1090, 2011-09-01
NAID 10031141041

Visualization of Phosphoinositides via the Development of the Transient Expression System of a Cyan Fluorescent Protein in the Red Alga Porphyra yezoensis