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2mkh

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Revision as of 21:43, 11 September 2015

Solution structure of tandem RRM domains of cytoplasmic polyadenylation element binding protein 1 (CPEB1) in free state

Structural highlights

2mkh is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2mke, 2mki, 2mkj, 2mkk
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CPEB1_HUMAN] Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation (By similarity). Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses (By similarity). Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation (By similarity). Induces the assembly of stress granules in the absence of stress.^[1] ^[2]

Publication Abstract from PubMed

Cytoplasmic changes in polyA tail length is a key mechanism of translational control and is implicated in germline development, synaptic plasticity, cellular proliferation, senescence, and cancer progression. The presence of a U-rich cytoplasmic polyadenylation element (CPE) in the 3' untranslated regions (UTRs) of the responding mRNAs gives them the selectivity to be regulated by the CPE-binding (CPEB) family of proteins, which recognizes RNA via the tandem RNA recognition motifs (RRMs). Here we report the solution structures of the tandem RRMs of two human paralogs (CPEB1 and CPEB4) in their free and RNA-bound states. The structures reveal an unprecedented arrangement of RRMs in the free state that undergo an original closure motion upon RNA binding that ensures high fidelity. Structural and functional characterization of the ZZ domain (zinc-binding domain) of CPEB1 suggests a role in both protein-protein and protein-RNA interactions. Together with functional studies, the structures reveal how RNA binding by CPEB proteins leads to an optimal positioning of the N-terminal and ZZ domains at the 3' UTR, which favors the nucleation of the functional ribonucleoprotein complexes for translation regulation.

A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins.,Afroz T, Skrisovska L, Belloc E, Guillen-Boixet J, Mendez R, Allain FH Genes Dev. 2014 Jul 1;28(13):1498-514. doi: 10.1101/gad.241133.114. PMID:24990967^[3]

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

References

↑ Sasayama T, Marumoto T, Kunitoku N, Zhang D, Tamaki N, Kohmura E, Saya H, Hirota T. Over-expression of Aurora-A targets cytoplasmic polyadenylation element binding protein and promotes mRNA polyadenylation of Cdk1 and cyclin B1. Genes Cells. 2005 Jul;10(7):627-38. PMID:15966895 doi:10.1111/j.1365-2443.2005.00870.x
↑ Wilczynska A, Aigueperse C, Kress M, Dautry F, Weil D. The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules. J Cell Sci. 2005 Mar 1;118(Pt 5):981-92. PMID:15731006 doi:118/5/981
↑ Afroz T, Skrisovska L, Belloc E, Guillen-Boixet J, Mendez R, Allain FH. A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins. Genes Dev. 2014 Jul 1;28(13):1498-514. doi: 10.1101/gad.241133.114. PMID:24990967 doi:http://dx.doi.org/10.1101/gad.241133.114

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mkh"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[2mkh]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MKH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MKH FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mke|2mke]], [[2mki|2mki]], [[2mkj|2mkj]], [[2mkk|2mkk]]</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=2mkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mkh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mkh RCSB], [http://www.ebi.ac.uk/pdbsum/2mkh 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=2mkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mkh OCA], [http://pdbe.org/2mkh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mkh RCSB], [http://www.ebi.ac.uk/pdbsum/2mkh PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2mkh" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2mkh

From Proteopedia

Revision as of 21:43, 11 September 2015

Solution structure of tandem RRM domains of cytoplasmic polyadenylation element binding protein 1 (CPEB1) in free state

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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