5k6s

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The structure of the PP2A B56 subunit BubR1 complex

Structural highlights

5k6s is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.794Å
Ligands:SEP
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

2A5G_HUMAN The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.[1] [2]

Publication Abstract from PubMed

Specific interactions between proteins govern essential physiological processes including signaling. Many enzymes, especially the family of serine/threonine phosphatases (PSPs: PP1, PP2A, and PP2B/calcineurin/CN), recruit substrates and regulatory proteins by binding short linear motifs (SLiMs), short sequences found within intrinsically disordered regions that mediate specific protein-protein interactions. While tremendous progress had been made in identifying where and how SLiMs bind PSPs, especially PP1 and CN, essentially nothing is known about how SLiMs bind PP2A, a validated cancer drug target. Here we describe three structures of a PP2A-SLiM interaction (B56:pS-RepoMan, B56:pS-BubR1, and B56:pSpS-BubR1), show that this PP2A-specific SLiM is defined as LSPIxE, and then use these data to discover scores of likely PP2A regulators and substrates. Together, these data provide a powerful approach not only for dissecting PP2A interaction networks in cells but also for targeting PP2A diseases, such as cancer.

Expanding the PP2A Interactome by Defining a B56-Specific SLiM.,Wang X, Bajaj R, Bollen M, Peti W, Page R Structure. 2016 Dec 6;24(12):2174-2181. doi: 10.1016/j.str.2016.09.010. Epub 2016, Oct 27. PMID:27998540[3]

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

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

See Also

References

  1. ↑ Letourneux C, Rocher G, Porteu F. B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK. EMBO J. 2006 Feb 22;25(4):727-38. Epub 2006 Feb 2. PMID:16456541 doi:http://dx.doi.org/10.1038/sj.emboj.7600980
  2. ↑ Li HH, Cai X, Shouse GP, Piluso LG, Liu X. A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55. EMBO J. 2007 Jan 24;26(2):402-11. PMID:17245430 doi:http://dx.doi.org/10.1038/sj.emboj.7601519
  3. ↑ Wang X, Bajaj R, Bollen M, Peti W, Page R. Expanding the PP2A Interactome by Defining a B56-Specific SLiM. Structure. 2016 Dec 6;24(12):2174-2181. doi: 10.1016/j.str.2016.09.010. Epub 2016, Oct 27. PMID:27998540 doi:http://dx.doi.org/10.1016/j.str.2016.09.010

Contents


PDB ID 5k6s

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