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| {{#tree:id=OrganizedByTopic|openlevels=0| | | {{#tree:id=OrganizedByTopic|openlevels=0| |
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| | *Protein phosphatase 1 |
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| | **[[2rlt]] - PP1 regulatory subunit - pig - NMR<br /> |
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| *Protein phosphatase 1A | | *Protein phosphatase 1A |
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| **[[3fxj]], [[3fxk]], [[3fxl]], [[3fxm]], [[3fxo]], [[4ra2]] – hPP1A + Mn – human<br /> | | **[[3fxj]], [[3fxk]], [[3fxl]], [[3fxm]], [[3fxo]], [[4ra2]] – hPP1A + Mn – human<br /> |
| **[[4da1]] – hPP1K + Mn<br />
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| **[[3n5u]] – hPP1A catalytic subunit + retinoblastoma-associated protein<br /> | | **[[3n5u]] – hPP1A catalytic subunit + retinoblastoma-associated protein<br /> |
| **[[3v4y]] – hPP1A catalytic subunit + PP1 nuclear inhibitor<br />
| |
| **[[4g9j]], [[5ioh]] – hPP1A catalytic subunit + peptide<br /> | | **[[4g9j]], [[5ioh]] – hPP1A catalytic subunit + peptide<br /> |
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| | *Protein phosphatase 1G |
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| **[[5inb]], [[5j28]] - hPP1G catalytic subunit + peptide<br /> | | **[[5inb]], [[5j28]] - hPP1G catalytic subunit + peptide<br /> |
| **[[2rlt]] – PP1 regulatory subunit – pig - NMR<br /> | | |
| | *Protein phosphatase 1K |
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| | **[[4da1]] - hPP1K + Mn<br /> |
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| *Protein phosphatase 2A | | *Protein phosphatase 2A |
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| **[[2iq1]] – hPP2C κ <br /> | | **[[2iq1]] – hPP2C κ <br /> |
| | **[[4raf]], [[4rag]] - hPP2C α (mutant) + Mn<br /> |
| **[[3d8k]] – PP2C – ''Toxoplasma gondii''<br /> | | **[[3d8k]] – PP2C – ''Toxoplasma gondii''<br /> |
| **[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 – ''Arabidopsis thaliana''<br /> | | **[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 + pyrabactin – ''Arabidopsis thaliana''<br /> |
| | **[[3kdj]] - AtPP2C + Pyl1 + abscicic acid<br /> |
| **[[3nmt]], [[3kb3]], [[3nmv]], [[3ujl]] – AtPP2C + Pyl2<br /> | | **[[3nmt]], [[3kb3]], [[3nmv]], [[3ujl]] – AtPP2C + Pyl2<br /> |
| **[[4la7]], [[4lg5]], [[4lga]], [[4lgb]] – AtPP2C + Pyl2 + ligand<br /> | | **[[4la7]], [[4lg5]], [[4lga]], [[4lgb]] – AtPP2C + Pyl2 + ligand<br /> |
| **[[4ds8]] – AtPP2C + Pyl3 + Mn<br /> | | **[[4ds8]], [[5jo1]], [[5jo2]] – AtPP2C + Pyl3 + Mn<br /> |
| **[[3rt0]] – AtPP2C (mutant) + Pyl10<br /> | | **[[3rt0]] – AtPP2C (mutant) + Pyl10<br /> |
| **[[4n0g]] – AtPP2C + Pyl13<br /> | | **[[4n0g]] – AtPP2C + Pyl13<br /> |
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| **[[4yzg]] – AtPP2C (mutant) <br /> | | **[[4yzg]] – AtPP2C (mutant) <br /> |
| **[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br /> | | **[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br /> |
| | | **[[3ujg]] - AtPP2C + SRK2E<br /> |
| }} | | }} |
| == References == | | == References == |
| <references/> | | <references/> |
| [[Category:Topic Page]] | | [[Category:Topic Page]] |
| Function
Protein phosphatases (PP) regulate protein phosphorylation and thus are key in intracellular signal transduction processes.
- PP1 is a serine/threonine phosphatase and is a key component of the insulin signaling pathway[1].
- PP2A targets proteins in the oncogenic signaling pathways[2]. For PP2A see also HEAT Repeat.
- 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.
- PP4 regulates a variety of cellular functions[3].
- PP5 is activated by lipids and is involved in signal transduction[4].
Disease
Mutations in PP2A are found in many solid cancers and leukemias. PP2A-activating drugs are possible candidates for cancer therapeutics protocols[5]. Development of Alzheimer disease drugs could be based on restoration of PP2A activity[6].
Structural highlights
Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin. Algal toxin binds at the surface pocket of the PP2A catalytic subunit which contains the Mn+2 ion cofactors[7]. Water molecule shown as red sphere.
- ↑ 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:https://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:https://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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3D Structures of protein phosphatase
Updated on 21-September-2017
{"openlevels":0}
- Protein phosphatase 1
- Protein phosphatase 1A
- Protein phosphatase 1G
- 5inb, 5j28 - hPP1G catalytic subunit + peptide
- Protein phosphatase 1K
- Protein phosphatase 2A
- 1b3u, 2g62, 2hv6 – hPP2A regulatory subunit
- 2ie3, 2ie4, 2npp, 2nyl, 2nym – hPP2A catalytic + regulatory subunit + tumor-inducing toxin
- 3c5w – hPP2A catalytic + regulatory subunit + PP2A-specific methyltransferase
- Protein phosphatase 2C
- 2iq1 – hPP2C κ
- 4raf, 4rag - hPP2C α (mutant) + Mn
- 3d8k – PP2C – Toxoplasma gondii
- 3jrq, 3nmn – AtPP2C + Pyl1 + pyrabactin – Arabidopsis thaliana
- 3kdj - AtPP2C + Pyl1 + abscicic acid
- 3nmt, 3kb3, 3nmv, 3ujl – AtPP2C + Pyl2
- 4la7, 4lg5, 4lga, 4lgb – AtPP2C + Pyl2 + ligand
- 4ds8, 5jo1, 5jo2 – AtPP2C + Pyl3 + Mn
- 3rt0 – AtPP2C (mutant) + Pyl10
- 4n0g – AtPP2C + Pyl13
- 3qn1, 3zvu, 4wvo – AtPP2C + Pyr1
- 3ujk – AtPP2C
- 4yzg – AtPP2C (mutant)
- 4yzh – AtPP2C (mutant) + chlorophyll-binding protein peptide
- 3ujg - AtPP2C + SRK2E
References