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Phospholipase C

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== Function ==
== Function ==
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'''Phospholipase C''' (PLC) cleaves phospholipids before the phosphate group.
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'''Phospholipase C β,γ,δ,ε''' catalyze the conversion of phosphatidylinositol 4,5-bisphosphate to inositol 1,4,5-trisphosphate and diacylglycerol.<ref>PMID:12054652</ref>
'''Phosphatidylinositol-specific phospholipase C''' (PIPLC) catalyzes the hydrolysis of phosphatidylinositol into inositol triphosphate and deacylglycerol. PIPLC functions at the plasma membrane. PIPLC can release phosphatidylinositol-linked proteins (i.e., acetylcholinesterase) from the membrane by enzymatically cleaving their GPI anchor.
'''Phosphatidylinositol-specific phospholipase C''' (PIPLC) catalyzes the hydrolysis of phosphatidylinositol into inositol triphosphate and deacylglycerol. PIPLC functions at the plasma membrane. PIPLC can release phosphatidylinositol-linked proteins (i.e., acetylcholinesterase) from the membrane by enzymatically cleaving their GPI anchor.
== Disease ==
== Disease ==
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Phospholipase C γ gene blocking can stop breast cancer.<ref>PMID:19074886</ref> Phospholipase C δ has important suppressive role in the development and progression of esophageal carcinoma.
== Relevance ==
== Relevance ==
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**[[1aod]] – LmPIPLC + myo-inositol <br />
**[[1aod]] – LmPIPLC + myo-inositol <br />
**[[3ea2]] – BtPIPLC + myo-inositol <br />
**[[3ea2]] – BtPIPLC + myo-inositol <br />
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**[[3v16]], [[4f2b]] – SaPIPLC + myo-inositol <br />
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**[[3v16]], [[4f2b]], [[4rv3]] – SaPIPLC + myo-inositol <br />
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**[[3v1h]], [[4i9t]] – SaPIPLC (mutant) + myo-inositol <br />
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**[[3v1h]], [[4i9t]], [[4s3g]] – SaPIPLC (mutant) + myo-inositol <br />
**[[4i90]] – SaPIPLC (mutant) + choline <br />
**[[4i90]] – SaPIPLC (mutant) + choline <br />
**[[4i9j]] – SaPIPLC (mutant) + diC4PC <br />
**[[4i9j]] – SaPIPLC (mutant) + diC4PC <br />
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* Phospholipase C β
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**[[1jad]] – PLCB - turkey<br />
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**[[2zkm]] – hPLCB-2 - human<br />
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**[[2fju]] – hPLCB-2 + RAC1<br />
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**[[3ohm]], [[4gnk]], [[4qj3]] – hPLCB-3 + guanine nucleotide-binding protein G subunit alpha<br />
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**[[4qj4]], [[4qj5]] – hPLCB-3 + guanine nucleotide-binding protein G subunit alpha + inositol phosphate derivative <br />
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**[[3qr0]] – PLCB - cuttlefish<br />
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**[[3qr1]] – PLCB - squid<br />
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* Phospholipase C γ
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**[[1hsq]], [[2hsp]] – hPLCG SH3 domain - NMR <br />
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**[[4fbn]] – hPLCG-1<br />
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**[[2k2j]] – hPLCG-2 split PH2 domain - NMR<br />
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**[[2w2w]] – hPLCG-2 split PH2 domain (mutant)<br />
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**[[2w2x]] – hPLCG-2 split PH2 domain + RAC2 br />
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**[[4ey0]] – hPLCG-1 SH2 domain (mutant)<br />
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**[[2pld]], [[2ple]] – PLCG C terminal SH2 domain + PDGF peptide – bovine - NMR <br />
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**[[1ywp]] – rPLCG-1 SH3 domain – rat<br />
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**[[1y0m]] – rPLCG-1 SH3 domain (mutant)<br />
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**[[2fjl]] – rPLCG-1 split PH2 domain - NMR<br />
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**[[2eob]] – rPLCG-2 SH2 domain - NMR<br />
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**[[1ywo]] – rPLCG-1 SH3 domain + lymphocyte cytosolic protein peptide <br />
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**[[4k44]], [[4k45]] – rPLCG C terminal SH2 domain <br />
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**[[2dx0]] – mPLCG-2 N terminal SH2 domain – mouse<br />
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**[[2eqi]] – mPLCG-2 SH3 domain - NMR<br />
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* Phospholipase C δ
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**[[1mai]] – rPLCD-1 PH domain + inositol triphosphate <br />
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**[[1qas]], [[1qat]], [[1djg]], [[1djh]], [[1dji]], [[2isd]] – rPLCD-1 <br />
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**[[1djx]], [[1djy]] – rPLCD-1 + inositol triphosphate <br />
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**[[1djz]], [[1djw]] – rPLCD-1 + inositol phosphate derivative <br />
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* Phospholipase C ε
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**[[2bye]] – hPLCE-1 RA1 domain - NMR <br />
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**[[2byf]] – hPLCE-1 RA2 domain - NMR <br />
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* Phospholipase C
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**[[1ah7]] – BcPLC<br />
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**[[1p5x]], [[2ffz]], [[2fgn]], [[2huc]] – BcPLC (mutant)<br />
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**[[1p6d]], [[1p6e]] – BcPLC (mutant) + phosphocholine derivative <br />
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**[[1ca1]], [[1qm6]], [[1qmd]], [[1gyg]], [[1kho]], [[2wxt]] – CpPLC – Clostridium perfringensbr />
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**[[2wxu]], [[2wy6]] – CpPLC (mutant)<br />
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}}
}}

Revision as of 09:56, 10 January 2016

Structure of phosphatidylinositol-specific phospholipase C complex with myo-inositol (PDB code 1ptg).

Drag the structure with the mouse to rotate

3D structures of phosphatidylinositol-specific phospholipase C

Updated on 10-January-2016

References

  1. ↑ Barr AJ, Marjoram R, Xu J, Snyderman R. Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3. Biochem Biophys Res Commun. 2002 Apr 26;293(1):647-52. PMID:12054652 doi:http://dx.doi.org/10.1016/S0006-291X(02)00259-0
  2. ↑ Sala G, Dituri F, Raimondi C, Previdi S, Maffucci T, Mazzoletti M, Rossi C, Iezzi M, Lattanzio R, Piantelli M, Iacobelli S, Broggini M, Falasca M. Phospholipase Cgamma1 is required for metastasis development and progression. Cancer Res. 2008 Dec 15;68(24):10187-96. doi: 10.1158/0008-5472.CAN-08-1181. PMID:19074886 doi:http://dx.doi.org/10.1158/0008-5472.CAN-08-1181

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