4wsf

From Proteopedia

(Difference between revisions)

Revision as of 18:23, 11 August 2016

Falafel EVH1 domain bound to CENP-C FIM

Structural highlights

4wsf is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
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.

References

↑ 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
↑ 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
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4wsf"

Categories: Lefevre, S R | Singleton, M R | Phosphatase evh1 domain | Signaling protein

@@ Line 1: / Line 1: @@
 ==Falafel EVH1 domain bound to CENP-C FIM==
 <StructureSection load='4wsf' size='340' side='right' caption='[[4wsf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4wsf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WSF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WSF FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wsf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wsf RCSB], [http://www.ebi.ac.uk/pdbsum/4wsf PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wsf OCA], [http://pdbe.org/4wsf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wsf RCSB], [http://www.ebi.ac.uk/pdbsum/4wsf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wsf ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4wsf" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Serine/threonine protein phosphatase|Serine/threonine protein phosphatase]]
 == References ==
 <references/>

4wsf

From Proteopedia

Revision as of 18:23, 11 August 2016

Falafel EVH1 domain bound to CENP-C FIM

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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