Protein phosphatase: Difference between revisions

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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|
   
   
*Protein phosphatase 1
**[[2rlt]] - PP1 regulatory subunit - pig - NMR<br />
*Protein phosphatase 1A
*Protein phosphatase 1A


**[[3fxj]], [[3fxk]], [[3fxl]], [[3fxm]], [[3fxo]], [[4ra2]] – hPP1A + Mn – human<br />
**[[3fxj]], [[3fxk]], [[3fxl]], [[3fxm]], [[3fxo]], [[4ra2]] – hPP1A + Mn – human<br />
**[[4da1]] – hPP1K + Mn<br />
**[[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 />
*Protein phosphatase 1G
**[[5inb]], [[5j28]] - hPP1G catalytic subunit + peptide<br />
**[[5inb]], [[5j28]] - hPP1G catalytic subunit + peptide<br />
**[[2rlt]] – PP1 regulatory subunit – pig - NMR<br />
 
*Protein phosphatase 1K
 
**[[4da1]] - hPP1K + Mn<br />


*Protein phosphatase 2A
*Protein phosphatase 2A
Line 40: Line 48:


**[[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]]

Revision as of 21:26, 21 September 2017

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

. 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.

  • .
  • .

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

Drag the structure with the mouse to rotate

3D Structures of protein phosphatase3D Structures of protein phosphatase

Updated on 21-September-2017

ReferencesReferences

  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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Alexsandra Tifane Santos do Nascimento
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