Protein phosphatase
From Proteopedia
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| - | <StructureSection load=' | + | <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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== Function == | == Function == | ||
| - | '''Protein phosphatases''' (PP) regulate protein phosphorylation and thus are key in intracellular signal transduction processes.<br /> | + | '''Protein phosphatases''' (PP) or '''serine/threonine protein phosphatase''' regulate protein phosphorylation and thus are key in intracellular signal transduction processes.<br /> |
| - | * '''PP1''' is a serine/threonine phosphatase and is a key component of the insulin signaling pathway<ref>PMID:9609113</ref>.<br /> | + | * '''PP1''' is a serine/threonine phosphatase and is a key component of the insulin signaling pathway<ref>PMID:9609113</ref>.<br /> |
| + | * '''PP1C''' is the catalytic subunit of PP1. | ||
| + | * '''PP1K''' is Mn+2/Mg+2-dependent PP1. | ||
* '''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 /> | ||
| - | * '''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 /> | + | * '''PP2C''' are Mg/Mn-dependent and are essential for the regulation of cell cycle and stress signaling pathways. For details see<br /> |
| + | * <scene name='54/540142/Protein_pp2cm_with_mgii/4'>PP2Cm</scene> | ||
| + | *[[Protein Phosphatase 2C]]<br /> | ||
| + | *[[ABA-regulated Protein Phosphatase 2C]]<br /> | ||
| + | *[[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 == | ||
| - | <scene name='54/540142/Cv/ | + | <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. |
| - | *<scene name='54/540142/Cv/ | + | *<scene name='54/540142/Cv/6'>Mn+2 ion cofactors coordination site</scene>. |
| - | *<scene name='54/540142/Cv/ | + | *<scene name='54/540142/Cv/7'>Whole binding site</scene>. |
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== 3D Structures of protein phosphatase== | == 3D Structures of protein phosphatase== | ||
| - | + | [[Protein phosphatase 3D structures]] | |
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| - | + | </StructureSection> | |
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| - | **[[2iq1]] – hPP2C κ <br /> | ||
| - | **[[4raf]], [[4rag]] - hPP2C α (mutant) + Mn<br /> | ||
| - | **[[3d8k]] – PP2C – ''Toxoplasma gondii''<br /> | ||
| - | **[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 + pyrabactin – ''Arabidopsis thaliana''<br /> | ||
| - | **[[3kdj]] - AtPP2C + Pyl1 + abscicic acid<br /> | ||
| - | **[[3nmt]], [[3kb3]], [[3nmv]], [[3ujl]] – AtPP2C + Pyl2<br /> | ||
| - | **[[4la7]], [[4lg5]], [[4lga]], [[4lgb]] – AtPP2C + Pyl2 + ligand<br /> | ||
| - | **[[4ds8]], [[5jo1]], [[5jo2]] – AtPP2C + Pyl3 + Mn<br /> | ||
| - | **[[3rt0]] – AtPP2C (mutant) + Pyl10<br /> | ||
| - | **[[4n0g]] – AtPP2C + Pyl13<br /> | ||
| - | **[[3qn1]], [[3zvu]], [[4wvo]] – AtPP2C + Pyr1<br /> | ||
| - | **[[3ujk]] – AtPP2C <br /> | ||
| - | **[[4yzg]] – AtPP2C (mutant) <br /> | ||
| - | **[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br /> | ||
| - | **[[3ujg]] - AtPP2C + SRK2E<br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Ragolia L, Begum N. Protein phosphatase-1 and insulin action. Mol Cell Biochem. 1998 May;182(1-2):49-58. PMID:9609113
- ↑ 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
- ↑ 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
- ↑ Chinkers M. Protein phosphatase 5 in signal transduction. Trends Endocrinol Metab. 2001 Jan-Feb;12(1):28-32. PMID:11137038
- ↑ 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
- ↑ Rudrabhatla P, Pant HC. Role of protein phosphatase 2A in Alzheimer's disease. Curr Alzheimer Res. 2011 Sep;8(6):623-32. PMID:21605044
- ↑ 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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