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'''Phospholipase D2''' is an [[enzyme]] that in humans is encoded by the ''PLD2'' [[gene]].<ref name="pmid9858823">{{cite journal | vauthors = Park SH, Ryu SH, Suh PG, Kim H | title = Assignment of human PLD2 to chromosome band 17p13.1 by fluorescence in situ hybridization | journal = Cytogenet Cell Genet | volume = 82 | issue = 3–4 | pages = 225 | date = February 1999 | pmid = 9858823 | pmc =  | doi = 10.1159/000015106 }}</ref><ref name="pmid9582313">{{cite journal | vauthors = Lopez I, Arnold RS, Lambeth JD | title = Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2 | journal = J Biol Chem | volume = 273 | issue = 21 | pages = 12846–52 | date = June 1998 | pmid = 9582313 | pmc = | doi = 10.1074/jbc.273.21.12846 }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Phospholipase D2
| HGNCid = 9068
| Symbol = PLD2
| AltSymbols =;
| OMIM = 602384
| ECnumber = 
| Homologene = 55672
| MGIid = 892877
| GeneAtlas_image1 = PBB_GE_PLD2_209643_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0004630 |text = phospholipase D activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0035091 |text = phosphoinositide binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0002031 |text = G-protein coupled receptor internalization}} {{GNF_GO|id=GO:0006898 |text = receptor-mediated endocytosis}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0007154 |text = cell communication}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5338
    | Hs_Ensembl = ENSG00000129219
    | Hs_RefseqProtein = NP_002654
    | Hs_RefseqmRNA = NM_002663
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 4657348
    | Hs_GenLoc_end = 4673694
    | Hs_Uniprot = O14939
    | Mm_EntrezGene = 18806
    | Mm_Ensembl = ENSMUSG00000020828
    | Mm_RefseqmRNA = NM_008876
    | Mm_RefseqProtein = NP_032902
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 70356359
    | Mm_GenLoc_end = 70374305
    | Mm_Uniprot = Q3UNY4
  }}
}}
'''Phospholipase D2''', also known as '''PLD2''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Phosphatidylcholine]] (PC)-specific [[phospholipase D|phospholipases D]] (PLDs) catalyze the hydrolysis of PC to produce [[phosphatidic acid]] and [[choline]]. Activation of PC-specific PLDs occurs as a consequence of agonist stimulation of both [[tyrosine kinase]] and [[G protein-coupled receptor]]s. PC-specific PLDs have been proposed to function in regulated secretion, cytoskeletal reorganization, transcriptional regulation, and cell cycle control.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PLD2 phospholipase D2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5338}}</ref>
{{PBB_Summary
| section_title =
| summary_text = Phosphatidylcholine (PC)-specific phospholipases D (PLDs) catalyze the hydrolysis of PC to produce phosphatidic acid and choline. Activation of PC-specific PLDs occurs as a consequence of agonist stimulation of both tyrosine kinase and G protein-coupled receptors. PC-specific PLDs have been proposed to function in regulated secretion, cytoskeletal reorganization, transcriptional regulation, and cell cycle control.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PLD2 phospholipase D2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5338| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
PLD2 has been shown to [[Protein-protein interaction|interact]] with:
{{refbegin | 2}}
{{div col|colwidth=20em}}
{{PBB_Further_reading
* [[ARF1]],<ref name = pmid11373276>{{cite journal | vauthors = Lee S, Park JB, Kim JH, Kim Y, Kim JH, Shin KJ, Lee JS, Ha SH, Suh PG, Ryu SH | title = Actin directly interacts with phospholipase D, inhibiting its activity | journal = J. Biol. Chem. | volume = 276 | issue = 30 | pages = 28252–60 | date = July 2001 | pmid = 11373276 | doi = 10.1074/jbc.M008521200 }}</ref><ref name = pmid10801846>{{cite journal | vauthors = Park JB, Kim JH, Kim Y, Ha SH, Yoo JS, Du G, Frohman MA, Suh PG, Ryu SH | title = Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner | journal = J. Biol. Chem. | volume = 275 | issue = 28 | pages = 21295–301 | date = July 2000 | pmid = 10801846 | doi = 10.1074/jbc.M002463200 }}</ref>
| citations =  
* [[Aldolase A]],<ref name = pmid11876650>{{cite journal | vauthors = Kim JH, Lee S, Kim JH, Lee TG, Hirata M, Suh PG, Ryu SH | title = Phospholipase D2 directly interacts with aldolase via Its PH domain | journal = Biochemistry | volume = 41 | issue = 10 | pages = 3414–21 | date = March 2002 | pmid = 11876650 | doi =  10.1021/bi015700a}}</ref>
*{{cite journal  | author=Sundaram M, Cook HW, Byers DM |title=The MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular components. |journal=Biochem. Cell Biol. |volume=82 |issue= 1 |pages= 191-200 |year= 2004 |pmid= 15052337 |doi= 10.1139/o03-087 }}
* [[Amphiphysin]],<ref name = pmid10764771/>
*{{cite journal | author=McDermott M, Wakelam MJ, Morris AJ |title=Phospholipase D. |journal=Biochem. Cell Biol. |volume=82 |issue= 1 |pages= 225-53 |year= 2004 |pmid= 15052340 |doi= 10.1139/o03-079 }}
* [[BIN1]],<ref name = pmid10764771>{{cite journal | vauthors = Lee C, Kim SR, Chung JK, Frohman MA, Kilimann MW, Rhee SG | title = Inhibition of phospholipase D by amphiphysins | journal = J. Biol. Chem. | volume = 275 | issue = 25 | pages = 18751–8 | date = June 2000 | pmid = 10764771 | doi = 10.1074/jbc.M001695200 }}</ref>
*{{cite journal | author=Colley WC, Sung TC, Roll R, ''et al.'' |title=Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization. |journal=Curr. Biol. |volume=7 |issue= 3 |pages= 191-201 |year= 1997 |pmid= 9395408 |doi=  }}
* [[Caveolin 1]],<ref name = pmid14675200>{{cite journal | vauthors = Zheng X, Bollinger Bollag W | title = Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane microdomains and is downregulated upon keratinocyte differentiation | journal = J. Invest. Dermatol. | volume = 121 | issue = 6 | pages = 1487–95 | date = December 2003 | pmid = 14675200 | doi = 10.1111/j.1523-1747.2003.12614.x }}</ref><ref name = pmid10675563>{{cite journal | vauthors = Czarny M, Fiucci G, Lavie Y, Banno Y, Nozawa Y, Liscovitch M | title = Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains | journal = FEBS Lett. | volume = 467 | issue = 2-3 | pages = 326–32 | date = February 2000 | pmid = 10675563 | doi =  10.1016/s0014-5793(00)01174-1}}</ref>
*{{cite journal | author=Lopez I, Arnold RS, Lambeth JD |title=Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. |journal=J. Biol. Chem. |volume=273 |issue= 21 |pages= 12846-52 |year= 1998 |pmid= 9582313 |doi= }}
* [[Glyceraldehyde 3-phosphate dehydrogenase]],<ref name = pmid12753082>{{cite journal | vauthors = Kim JH, Lee S, Park JB, Lee SD, Kim JH, Ha SH, Hasumi K, Endo A, Suh PG, Ryu SH | title = Hydrogen peroxide induces association between glyceraldehyde 3-phosphate dehydrogenase and phospholipase D2 to facilitate phospholipase D2 activation in PC12 cells | journal = J. Neurochem. | volume = 85 | issue = 5 | pages = 1228–36 | date = June 2003 | pmid = 12753082 | doi =  10.1046/j.1471-4159.2003.01755.x}}</ref>
*{{cite journal | author=Steed PM, Clark KL, Boyar WC, Lasala DJ |title=Characterization of human PLD2 and the analysis of PLD isoform splice variants. |journal=FASEB J. |volume=12 |issue= 13 |pages= 1309-17 |year= 1998 |pmid= 9761774 |doi= }}
* [[PLCG1]],<ref name = pmid12646582>{{cite journal | vauthors = Jang IH, Lee S, Park JB, Kim JH, Lee CS, Hur EM, Kim IS, Kim KT, Yagisawa H, Suh PG, Ryu SH | title = The direct interaction of phospholipase C-gamma 1 with phospholipase D2 is important for epidermal growth factor signaling | journal = J. Biol. Chem. | volume = 278 | issue = 20 | pages = 18184–90 | date = May 2003 | pmid = 12646582 | doi = 10.1074/jbc.M208438200 }}</ref>
*{{cite journal | author=Slaaby R, Jensen T, Hansen HS, ''et al.'' |title=PLD2 complexes with the EGF receptor and undergoes tyrosine phosphorylation at a single site upon agonist stimulation. |journal=J. Biol. Chem. |volume=273 |issue= 50 |pages= 33722-7 |year= 1999 |pmid= 9837959 |doi=  }}
* [[PRKCD]],<ref name = pmid11744693>{{cite journal | vauthors = Han JM, Kim JH, Lee BD, Lee SD, Kim Y, Jung YW, Lee S, Cho W, Ohba M, Kuroki T, Suh PG, Ryu SH | title = Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells | journal = J. Biol. Chem. | volume = 277 | issue = 10 | pages = 8290–7 | date = March 2002 | pmid = 11744693 | doi = 10.1074/jbc.M108343200 }}</ref>
*{{cite journal | author=Park SH, Ryu SH, Suh PG, Kim H |title=Assignment of human PLD2 to chromosome band 17p13.1 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=82 |issue= 3-4 |pages= 225 |year= 1999 |pmid= 9858823 |doi=  }}
* [[Src (gene)|Src]],<ref name = pmid12697812>{{cite journal | vauthors = Ahn BH, Kim SY, Kim EH, Choi KS, Kwon TK, Lee YH, Chang JS, Kim MS, Jo YH, Min DS | title = Transmodulation between phospholipase D and c-Src enhances cell proliferation | journal = Mol. Cell. Biol. | volume = 23 | issue = 9 | pages = 3103–15 | date = May 2003 | pmid = 12697812 | pmc = 153190 | doi = 10.1128/mcb.23.9.3103-3115.2003}}</ref>  and
*{{cite journal | author=Czarny M, Fiucci G, Lavie Y, ''et al.'' |title=Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains. |journal=FEBS Lett. |volume=467 |issue= 2-3 |pages= 326-32 |year= 2000 |pmid= 10675563 |doi= }}
* [[Wiskott-Aldrich syndrome protein]].<ref name = pmid21930784>{{cite journal | vauthors = Kantonen S, Hatton N, Mahankali M, Henkels KM, Park H, Cox D, Gomez-Cambronero J | title = A novel phospholipase D2-Grb2-WASp heterotrimer regulates leukocyte phagocytosis in a two-step mechanism | journal = Mol. Cell. Biol. | volume = 31 | issue = 22 | pages = 4524–37 | date = November 2011 | pmid = 21930784 | pmc = 3209255 | doi = 10.1128/MCB.05684-11 }}</ref>
*{{cite journal | author=Lee C, Kim SR, Chung JK, ''et al.'' |title=Inhibition of phospholipase D by amphiphysins. |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 18751-8 |year= 2000 |pmid= 10764771 |doi= 10.1074/jbc.M001695200 }}
{{Div col end}}
*{{cite journal | author=Park JB, Kim JH, Kim Y, ''et al.'' |title=Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21295-301 |year= 2000 |pmid= 10801846 |doi= 10.1074/jbc.M002463200 }}
 
*{{cite journal | author=Zhang Y, Redina O, Altshuller YM, ''et al.'' |title=Regulation of expression of phospholipase D1 and D2 by PEA-15, a novel protein that interacts with them. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 35224-32 |year= 2001 |pmid= 10926929 |doi= 10.1074/jbc.M003329200 }}
== Inhibitors ==
*{{cite journal  | author=Morash SC, Byers DM, Cook HW |title=Activation of phospholipase D by PKC and GTPgammaS in human neuroblastoma cells overexpressing MARCKS. |journal=Biochim. Biophys. Acta |volume=1487 |issue= 2-3 |pages= 177-89 |year= 2000 |pmid= 11018470 |doi= }}
* ''N''-(2-(1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)-2-naphthamide: 75-fold selective versus [[Phospholipase D1|PLD1]], IC<sub>50</sub> = 20 nM.<ref name="pmid20735042">{{cite journal | vauthors = Lavieri RR, Scott SA, Selvy PE, Kim K, Jadhav S, Morrison RD, Daniels JS, Brown HA, Lindsley CW | title = Design, Synthesis, and Biological Evaluation of Halogenated N-(2-(4-Oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)benzamides: Discovery of an Isoform-Selective Small Molecule Phospholipase D2 Inhibitor | journal = J. Med. Chem. | volume = 53 | issue = 18 | pages = 6706–19 | date = September 2010 | pmid = 20735042 | pmc = 3179181 | doi = 10.1021/jm100814g | url =  | issn =  }}</ref>
*{{cite journal | author=Divecha N, Roefs M, Halstead JR, ''et al.'' |title=Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity. |journal=EMBO J. |volume=19 |issue= 20 |pages= 5440-9 |year= 2000 |pmid= 11032811 |doi= 10.1093/emboj/19.20.5440 }}
{{Clear}}
*{{cite journal  | author=Slaaby R, Du G, Altshuller YM, ''et al.'' |title=Insulin-induced phospholipase D1 and phospholipase D2 activity in human embryonic kidney-293 cells mediated by the phospholipase C gamma and protein kinase C alpha signalling cascade. |journal=Biochem. J. |volume=351 Pt 3 |issue= |pages= 613-9 |year= 2001 |pmid= 11042115 |doi= }}
 
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
== References ==
*{{cite journal | author=Lee S, Park JB, Kim JH, ''et al.'' |title=Actin directly interacts with phospholipase D, inhibiting its activity. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 28252-60 |year= 2001 |pmid= 11373276 |doi= 10.1074/jbc.M008521200 }}
{{reflist|35em}}
*{{cite journal | author=Sarkar S, Miwa N, Kominami H, ''et al.'' |title=Regulation of mammalian phospholipase D2: interaction with and stimulation by G(M2) activator. |journal=Biochem. J. |volume=359 |issue= Pt 3 |pages= 599-604 |year= 2001 |pmid= 11672434 |doi=  }}
 
*{{cite journal | author=Denmat-Ouisse LA, Phebidias C, Honkavaara P, ''et al.'' |title=Regulation of constitutive protein transit by phospholipase D in HT29-cl19A cells. |journal=J. Biol. Chem. |volume=276 |issue= 52 |pages= 48840-6 |year= 2002 |pmid= 11687572 |doi= 10.1074/jbc.M104276200 }}
== Further reading ==
*{{cite journal | author=Lee S, Kim JH, Lee CS, ''et al.'' |title=Collapsin response mediator protein-2 inhibits neuronal phospholipase D(2) activity by direct interaction. |journal=J. Biol. Chem. |volume=277 |issue= 8 |pages= 6542-9 |year= 2002 |pmid= 11741937 |doi= 10.1074/jbc.M108047200 }}
{{refbegin|35em}}
*{{cite journal  | author=Han JM, Kim JH, Lee BD, ''et al.'' |title=Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8290-7 |year= 2002 |pmid= 11744693 |doi= 10.1074/jbc.M108343200 }}
* {{cite journal | vauthors = Sundaram M, Cook HW, Byers DM | title = The MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular components | journal = Biochem. Cell Biol. | volume = 82 | issue = 1 | pages = 191–200 | year = 2004 | pmid = 15052337 | doi = 10.1139/o03-087 }}
}}
* {{cite journal | vauthors = McDermott M, Wakelam MJ, Morris AJ | title = Phospholipase D | journal = Biochem. Cell Biol. | volume = 82 | issue = 1 | pages = 225–53 | year = 2004 | pmid = 15052340 | doi = 10.1139/o03-079 }}
* {{cite journal | vauthors = Colley WC, Sung TC, Roll R, Jenco J, Hammond SM, Altshuller Y, Bar-Sagi D, Morris AJ, Frohman MA | title = Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization | journal = Curr. Biol. | volume = 7 | issue = 3 | pages = 191–201 | year = 1997 | pmid = 9395408 | doi = 10.1016/S0960-9822(97)70090-3 }}
* {{cite journal | vauthors = Steed PM, Clark KL, Boyar WC, Lasala DJ | title = Characterization of human PLD2 and the analysis of PLD isoform splice variants | journal = FASEB J. | volume = 12 | issue = 13 | pages = 1309–17 | year = 1998 | pmid = 9761774 }}
* {{cite journal | vauthors = Slaaby R, Jensen T, Hansen HS, Frohman MA, Seedorf K | title = PLD2 complexes with the EGF receptor and undergoes tyrosine phosphorylation at a single site upon agonist stimulation | journal = J. Biol. Chem. | volume = 273 | issue = 50 | pages = 33722–7 | year = 1999 | pmid = 9837959 | doi = 10.1074/jbc.273.50.33722 }}
* {{cite journal | vauthors = Czarny M, Fiucci G, Lavie Y, Banno Y, Nozawa Y, Liscovitch M | title = Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains | journal = FEBS Lett. | volume = 467 | issue = 2–3 | pages = 326–32 | year = 2000 | pmid = 10675563 | doi = 10.1016/S0014-5793(00)01174-1 }}
* {{cite journal | vauthors = Lee C, Kim SR, Chung JK, Frohman MA, Kilimann MW, Rhee SG | title = Inhibition of phospholipase D by amphiphysins | journal = J. Biol. Chem. | volume = 275 | issue = 25 | pages = 18751–8 | year = 2000 | pmid = 10764771 | doi = 10.1074/jbc.M001695200 }}
* {{cite journal | vauthors = Park JB, Kim JH, Kim Y, Ha SH, Yoo JS, Du G, Frohman MA, Suh PG, Ryu SH | title = Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner | journal = J. Biol. Chem. | volume = 275 | issue = 28 | pages = 21295–301 | year = 2000 | pmid = 10801846 | doi = 10.1074/jbc.M002463200 }}
* {{cite journal | vauthors = Zhang Y, Redina O, Altshuller YM, Yamazaki M, Ramos J, Chneiweiss H, Kanaho Y, Frohman MA | title = Regulation of expression of phospholipase D1 and D2 by PEA-15, a novel protein that interacts with them | journal = J. Biol. Chem. | volume = 275 | issue = 45 | pages = 35224–32 | year = 2001 | pmid = 10926929 | doi = 10.1074/jbc.M003329200 }}
* {{cite journal | vauthors = Morash SC, Byers DM, Cook HW | title = Activation of phospholipase D by PKC and GTPgammaS in human neuroblastoma cells overexpressing MARCKS | journal = Biochim. Biophys. Acta | volume = 1487 | issue = 2–3 | pages = 177–89 | year = 2000 | pmid = 11018470 | doi = 10.1016/s1388-1981(00)00094-9 }}
* {{cite journal | vauthors = Divecha N, Roefs M, Halstead JR, D'Andrea S, Fernandez-Borga M, Oomen L, Saqib KM, Wakelam MJ, D'Santos C | title = Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity | journal = EMBO J. | volume = 19 | issue = 20 | pages = 5440–9 | year = 2000 | pmid = 11032811 | pmc = 314009 | doi = 10.1093/emboj/19.20.5440 }}
* {{cite journal | vauthors = Slaaby R, Du G, Altshuller YM, Frohman MA, Seedorf K | title = Insulin-induced phospholipase D1 and phospholipase D2 activity in human embryonic kidney-293 cells mediated by the phospholipase C gamma and protein kinase C alpha signalling cascade | journal = Biochem. J. | volume = 351 | issue = 3 | pages = 613–9 | year = 2001 | pmid = 11042115 | pmc = 1221400 | doi = 10.1042/0264-6021:3510613 }}
* {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Res. | volume = 10 | issue = 11 | pages = 1788–95 | year = 2001 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
* {{cite journal | vauthors = Lee S, Park JB, Kim JH, Kim Y, Kim JH, Shin KJ, Lee JS, Ha SH, Suh PG, Ryu SH | title = Actin directly interacts with phospholipase D, inhibiting its activity | journal = J. Biol. Chem. | volume = 276 | issue = 30 | pages = 28252–60 | year = 2001 | pmid = 11373276 | doi = 10.1074/jbc.M008521200 }}
* {{cite journal | vauthors = Sarkar S, Miwa N, Kominami H, Igarashi N, Hayashi S, Okada T, Jahangeer S, Nakamura S | title = Regulation of mammalian phospholipase D2: interaction with and stimulation by G(M2) activator | journal = Biochem. J. | volume = 359 | issue = Pt 3 | pages = 599–604 | year = 2001 | pmid = 11672434 | pmc = 1222181 | doi = 10.1042/0264-6021:3590599 }}
* {{cite journal | vauthors = Denmat-Ouisse LA, Phebidias C, Honkavaara P, Robin P, Geny B, Min DS, Bourgoin S, Frohman MA, Raymond MN | title = Regulation of constitutive protein transit by phospholipase D in HT29-cl19A cells | journal = J. Biol. Chem. | volume = 276 | issue = 52 | pages = 48840–6 | year = 2002 | pmid = 11687572 | doi = 10.1074/jbc.M104276200 }}
* {{cite journal | vauthors = Lee S, Kim JH, Lee CS, Kim JH, Kim Y, Heo K, Ihara Y, Goshima Y, Suh PG, Ryu SH | title = Collapsin response mediator protein-2 inhibits neuronal phospholipase D(2) activity by direct interaction | journal = J. Biol. Chem. | volume = 277 | issue = 8 | pages = 6542–9 | year = 2002 | pmid = 11741937 | doi = 10.1074/jbc.M108047200 }}
* {{cite journal | vauthors = Han JM, Kim JH, Lee BD, Lee SD, Kim Y, Jung YW, Lee S, Cho W, Ohba M, Kuroki T, Suh PG, Ryu SH | title = Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells | journal = J. Biol. Chem. | volume = 277 | issue = 10 | pages = 8290–7 | year = 2002 | pmid = 11744693 | doi = 10.1074/jbc.M108343200 }}
{{refend}}
{{refend}}


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[[Category:EC 3.1.4]]

Latest revision as of 18:16, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Phospholipase D2 is an enzyme that in humans is encoded by the PLD2 gene.[1][2]

Function

Phosphatidylcholine (PC)-specific phospholipases D (PLDs) catalyze the hydrolysis of PC to produce phosphatidic acid and choline. Activation of PC-specific PLDs occurs as a consequence of agonist stimulation of both tyrosine kinase and G protein-coupled receptors. PC-specific PLDs have been proposed to function in regulated secretion, cytoskeletal reorganization, transcriptional regulation, and cell cycle control.[supplied by OMIM][3]

Interactions

PLD2 has been shown to interact with:

Inhibitors

  • N-(2-(1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)-2-naphthamide: 75-fold selective versus PLD1, IC50 = 20 nM.[15]

References

  1. ↑ Park SH, Ryu SH, Suh PG, Kim H (February 1999). "Assignment of human PLD2 to chromosome band 17p13.1 by fluorescence in situ hybridization". Cytogenet Cell Genet. 82 (3–4): 225. doi:10.1159/000015106. PMID 9858823.
  2. ↑ Lopez I, Arnold RS, Lambeth JD (June 1998). "Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2". J Biol Chem. 273 (21): 12846–52. doi:10.1074/jbc.273.21.12846. PMID 9582313.
  3. ↑ "Entrez Gene: PLD2 phospholipase D2".
  4. ↑ Lee S, Park JB, Kim JH, Kim Y, Kim JH, Shin KJ, Lee JS, Ha SH, Suh PG, Ryu SH (July 2001). "Actin directly interacts with phospholipase D, inhibiting its activity". J. Biol. Chem. 276 (30): 28252–60. doi:10.1074/jbc.M008521200. PMID 11373276.
  5. ↑ Park JB, Kim JH, Kim Y, Ha SH, Yoo JS, Du G, Frohman MA, Suh PG, Ryu SH (July 2000). "Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner". J. Biol. Chem. 275 (28): 21295–301. doi:10.1074/jbc.M002463200. PMID 10801846.
  6. ↑ Kim JH, Lee S, Kim JH, Lee TG, Hirata M, Suh PG, Ryu SH (March 2002). "Phospholipase D2 directly interacts with aldolase via Its PH domain". Biochemistry. 41 (10): 3414–21. doi:10.1021/bi015700a. PMID 11876650.
  7. ↑ 7.0 7.1 Lee C, Kim SR, Chung JK, Frohman MA, Kilimann MW, Rhee SG (June 2000). "Inhibition of phospholipase D by amphiphysins". J. Biol. Chem. 275 (25): 18751–8. doi:10.1074/jbc.M001695200. PMID 10764771.
  8. ↑ Zheng X, Bollinger Bollag W (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane microdomains and is downregulated upon keratinocyte differentiation". J. Invest. Dermatol. 121 (6): 1487–95. doi:10.1111/j.1523-1747.2003.12614.x. PMID 14675200.
  9. ↑ Czarny M, Fiucci G, Lavie Y, Banno Y, Nozawa Y, Liscovitch M (February 2000). "Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains". FEBS Lett. 467 (2–3): 326–32. doi:10.1016/s0014-5793(00)01174-1. PMID 10675563.
  10. ↑ Kim JH, Lee S, Park JB, Lee SD, Kim JH, Ha SH, Hasumi K, Endo A, Suh PG, Ryu SH (June 2003). "Hydrogen peroxide induces association between glyceraldehyde 3-phosphate dehydrogenase and phospholipase D2 to facilitate phospholipase D2 activation in PC12 cells". J. Neurochem. 85 (5): 1228–36. doi:10.1046/j.1471-4159.2003.01755.x. PMID 12753082.
  11. ↑ Jang IH, Lee S, Park JB, Kim JH, Lee CS, Hur EM, Kim IS, Kim KT, Yagisawa H, Suh PG, Ryu SH (May 2003). "The direct interaction of phospholipase C-gamma 1 with phospholipase D2 is important for epidermal growth factor signaling". J. Biol. Chem. 278 (20): 18184–90. doi:10.1074/jbc.M208438200. PMID 12646582.
  12. ↑ Han JM, Kim JH, Lee BD, Lee SD, Kim Y, Jung YW, Lee S, Cho W, Ohba M, Kuroki T, Suh PG, Ryu SH (March 2002). "Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells". J. Biol. Chem. 277 (10): 8290–7. doi:10.1074/jbc.M108343200. PMID 11744693.
  13. ↑ Ahn BH, Kim SY, Kim EH, Choi KS, Kwon TK, Lee YH, Chang JS, Kim MS, Jo YH, Min DS (May 2003). "Transmodulation between phospholipase D and c-Src enhances cell proliferation". Mol. Cell. Biol. 23 (9): 3103–15. doi:10.1128/mcb.23.9.3103-3115.2003. PMC 153190. PMID 12697812.
  14. ↑ Kantonen S, Hatton N, Mahankali M, Henkels KM, Park H, Cox D, Gomez-Cambronero J (November 2011). "A novel phospholipase D2-Grb2-WASp heterotrimer regulates leukocyte phagocytosis in a two-step mechanism". Mol. Cell. Biol. 31 (22): 4524–37. doi:10.1128/MCB.05684-11. PMC 3209255. PMID 21930784.
  15. ↑ Lavieri RR, Scott SA, Selvy PE, Kim K, Jadhav S, Morrison RD, Daniels JS, Brown HA, Lindsley CW (September 2010). "Design, Synthesis, and Biological Evaluation of Halogenated N-(2-(4-Oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)benzamides: Discovery of an Isoform-Selective Small Molecule Phospholipase D2 Inhibitor". J. Med. Chem. 53 (18): 6706–19. doi:10.1021/jm100814g. PMC 3179181. PMID 20735042.

Further reading

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