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Protein phosphatase

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<StructureSection load='3k7v' size='400' side='right' scene='54/540142/Cv/1' caption='Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin and sulfate [[3k7v]]'>
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<StructureSection load='' size='350' side='right' scene='54/540142/Cv/1' caption='Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin and sulfate [[3k7v]]'>
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__TOC__
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== Function ==
== Function ==
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'''Protein phosphatases''' (PP) regulate protein phosphorylation and thus are key in intracellular signal transduction processes.<br />
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'''Protein phosphatases''' (PP) or '''serine/threonine protein phosphatase''' regulate protein phosphorylation and thus are key in intracellular signal transduction processes.<br />
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* '''PP1''' is a serine/threonine phosphatase and is a key component of the insulin signaling pathway<ref>PMID:9609113</ref>.<br />
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* '''PP1''' is a serine/threonine phosphatase and is a key component of the insulin signaling pathway<ref>PMID:9609113</ref>.<br />
* '''PP2A''' targets proteins in the oncogenic signaling pathways<ref>PMID:11812651</ref>. For PP2A see also [[HEAT Repeat]].<br />
* '''PP2A''' targets proteins in the oncogenic signaling pathways<ref>PMID:11812651</ref>. For PP2A see also [[HEAT Repeat]].<br />
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* '''PP2C''' are Mg/Mn- dependent and are essential for the regulation of cell cycle and stress signaling pathways. For details see [[ABA-regulated Protein Phosphatase 2C]].<br />
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* '''PP2C''' are Mg/Mn-dependent and are essential for the regulation of cell cycle and stress signaling pathways. For details see<br />
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* <scene name='54/540142/Protein_pp2cm_with_mgii/4'>PP2Cm</scene>
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*[[Protein Phosphatase 2C]]<br />
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*[[ABA-regulated Protein Phosphatase 2C]]<br />
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*[[ABA Signaling Pathway]].<br />
* '''PP4''' regulates a variety of cellular functions<ref>PMID:25562660</ref>.<br />
* '''PP4''' regulates a variety of cellular functions<ref>PMID:25562660</ref>.<br />
* '''PP5''' is activated by lipids and is involved in signal transduction<ref>PMID:11137038</ref>.
* '''PP5''' is activated by lipids and is involved in signal transduction<ref>PMID:11137038</ref>.
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== Structural highlights ==
== Structural highlights ==
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<scene name='54/540142/Cv/2'>Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin</scene>. Algal toxin binds at the surface pocket of the PP2A catalytic subunit which contains the Mn+2 ion cofactors<ref>PMID:19916524</ref>. Water molecule shown as red sphere.
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<scene name='54/540142/Cv/5'>Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin</scene>. Algal toxin binds at the surface pocket of the PP2A catalytic subunit which contains the Mn+2 ion cofactors<ref>PMID:19916524</ref>. Water molecule are shown as red sphere.
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*<scene name='54/540142/Cv/3'>Mn+2 ion cofactors coordination site</scene>.
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*<scene name='54/540142/Cv/6'>Mn+2 ion cofactors coordination site</scene>.
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*<scene name='54/540142/Cv/4'>Whole binding site</scene>.
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*<scene name='54/540142/Cv/7'>Whole binding site</scene>.
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</StructureSection>
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== 3D Structures of protein phosphatase==
== 3D Structures of protein phosphatase==
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[[Protein phosphatase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Protein phosphatase 1A
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**[[3fxj]], [[3fxk]], [[3fxl]], [[3fxm]], [[3fxo]], [[4ra2]] – hPP1A + Mn – human<br />
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</StructureSection>
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**[[4da1]] – hPP1K + Mn<br />
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**[[3n5u]] – hPP1A catalytic subunit + retinoblastoma-associated protein<br />
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**[[3v4y]] – hPP1A catalytic subunit + PP1 nuclear inhibitor<br />
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**[[4g9j]] – hPP1A catalytic subunit + peptide<br />
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**[[2rlt]] – PP1 regulatory subunit – pig - NMR<br />
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*Protein phosphatase 2A
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**[[1b3u]], [[2g62]] – hPP2A regulatory subunit <br />
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**[[2ie3]], [[2ie4]], [[2npp]], [[2nyl]], [[2nym]] – hPP2A catalytic + regulatory subunit + tumor-inducing toxin<br />
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**[[3c5w]] – hPP2A catalytic + regulatory subunit + PP2A-specific methyltransferase<br />
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*Protein phosphatase 2C
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**[[2iq1]] – hPP2C κ <br />
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**[[3d8k]] – PP2C – ''Toxoplasma gondii''<br />
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**[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 – ''Arabidopsis thaliana''<br />
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**[[3nmt]], [[3kb3]], [[3nmv]], [[3ujl]] – AtPP2C + Pyl2<br />
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**[[4la7]], [[4lg5]], [4lga]], [[4lgb]] – AtPP2C + Pyl2 + ligand<br />
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**[[4ds8]] – AtPP2C + Pyl3 + Mn<br />
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**[[3rt0]] – AtPP2C (mutant) + Pyl10<br />
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**[[4n0g]] – AtPP2C + Pyl13<br />
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**[[3qn1]], [[3zvu]], [[4wvo]] – AtPP2C + Pyr1<br />
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**[[3ujk]] – AtPP2C <br />
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**[[4yzg]] – AtPP2C (mutant) <br />
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**[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br />
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin and sulfate 3k7v

Drag the structure with the mouse to rotate

References

  1. ↑ Ragolia L, Begum N. Protein phosphatase-1 and insulin action. Mol Cell Biochem. 1998 May;182(1-2):49-58. PMID:9609113
  2. ↑ Resjo S, Goransson O, Harndahl L, Zolnierowicz S, Manganiello V, Degerman E. Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes. Cell Signal. 2002 Mar;14(3):231-8. PMID:11812651
  3. ↑ Lipinszki Z, Lefevre S, Savoian MS, Singleton MR, Glover DM, Przewloka MR. Centromeric binding and activity of Protein Phosphatase 4. Nat Commun. 2015 Jan 6;6:5894. doi: 10.1038/ncomms6894. PMID:25562660 doi:http://dx.doi.org/10.1038/ncomms6894
  4. ↑ Chinkers M. Protein phosphatase 5 in signal transduction. Trends Endocrinol Metab. 2001 Jan-Feb;12(1):28-32. PMID:11137038
  5. ↑ Perrotti D, Neviani P. Protein phosphatase 2A: a target for anticancer therapy. Lancet Oncol. 2013 May;14(6):e229-38. doi: 10.1016/S1470-2045(12)70558-2. PMID:23639323 doi:http://dx.doi.org/10.1016/S1470-2045(12)70558-2
  6. ↑ Rudrabhatla P, Pant HC. Role of protein phosphatase 2A in Alzheimer's disease. Curr Alzheimer Res. 2011 Sep;8(6):623-32. PMID:21605044
  7. ↑ Huhn J, Jeffrey PD, Larsen K, Rundberget T, Rise F, Cox NR, Arcus V, Shi Y, Miles CO. A structural basis for the reduced toxicity of dinophysistoxin-2. Chem Res Toxicol. 2009 Nov;22(11):1782-6. PMID:19916524 doi:10.1021/tx9001622
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