4wsf

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Falafel EVH1 domain bound to CENP-C FIM

Structural highlights

4wsf is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.501Å
Ligands:SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PP4R3_DROME Regulatory subunit of serine/threonine-protein phosphatase 4. The probable PP4 complex Pp4-19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is required to prevent caspase induced cell death (in vitro). May be involved in DNA damage repair. Key mediator specific for the localization of mira and associated cell fate determinants during both interphase and mitosis. Nuclear Flfl is required to exclude mira/pros from the nucleus when inefficiently bound to the cytoskeleton/cortex, whereas cytosolic or membrane-associated flfl is required for the cortical association and asymmetric localization of mira/pros/brat/stau at metaphase and anaphase.[1] [2] [3]

Publication Abstract from PubMed

The cell division cycle requires tight coupling between protein phosphorylation and dephosphorylation. However, understanding the cell cycle roles of multimeric protein phosphatases has been limited by the lack of knowledge of how their diverse regulatory subunits target highly conserved catalytic subunits to their sites of action. Phosphoprotein phosphatase 4 (PP4) has been recently shown to participate in the regulation of cell cycle progression. We now find that the EVH1 domain of the regulatory subunit 3 of Drosophila PP4, Falafel (Flfl), directly interacts with the centromeric protein C (CENP-C). Unlike other EVH1 domains that interact with proline-rich ligands, the crystal structure of the Flfl amino-terminal EVH1 domain bound to a CENP-C peptide reveals a new target-recognition mode for the phosphatase subunit. We also show that binding of Flfl to CENP-C is required to bring PP4 activity to centromeres to maintain CENP-C and attached core kinetochore proteins at chromosomes during mitosis.

Centromeric binding and activity of Protein Phosphatase 4.,Lipinszki Z, Lefevre S, Savoian MS, Singleton MR, Glover DM, Przewloka MR Nat Commun. 2015 Jan 6;6:5894. doi: 10.1038/ncomms6894. PMID:25562660[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
5 reviews cite this structure
Protein Serine/Threonine Phosphatases: Keys to Unlocking Regulators and Substrates.
Brautigan et al. (2018)
4 more
16 other articles
No citations found

See Also

References

  1. ↑ Gingras AC, Caballero M, Zarske M, Sanchez A, Hazbun TR, Fields S, Sonenberg N, Hafen E, Raught B, Aebersold R. A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity. Mol Cell Proteomics. 2005 Nov;4(11):1725-40. Epub 2005 Aug 5. PMID:16085932 doi:http://dx.doi.org/M500231-MCP200
  2. ↑ Martin-Granados C, Philp A, Oxenham SK, Prescott AR, Cohen PT. Depletion of protein phosphatase 4 in human cells reveals essential roles in centrosome maturation, cell migration and the regulation of Rho GTPases. Int J Biochem Cell Biol. 2008;40(10):2315-32. Epub 2008 Apr 8. PMID:18487071 doi:http://dx.doi.org/S1357-2725(08)00147-7
  3. ↑ Sousa-Nunes R, Chia W, Somers WG. Protein phosphatase 4 mediates localization of the Miranda complex during Drosophila neuroblast asymmetric divisions. Genes Dev. 2009 Feb 1;23(3):359-72. doi: 10.1101/gad.1723609. PMID:19204120 doi:http://dx.doi.org/10.1101/gad.1723609
  4. ↑ 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

Contents


PDB ID 4wsf

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OCA

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