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PRODID:Faculty of Science and Engineering - Research
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SUMMARY:CMCB Seminar - Prof Rebecca Page (UConn Health)
DESCRIPTION;ENCODING=QUOTED-PRINTABLE: Title: SLiMs and SHelMs: Decoding how short linear and helical motifs direct PPP specificity.=0D=0A=
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The large majority of ser/thr dephosphorylation is performed by the PPP family, comprised of just seven families: PP1, PP2A, PP2B/PP3/calcineurin (CN), PP4, PP5, PP6 and PP7. While it has been known for more than two decades that PP1 and CN engage their regulators using short linear motifs (SLiMs), the emerging view is that regulator and substrate engagement via SLiMs is likely conserved throughout the entire PPP family, with SLiMs now identified for PP4 and PP2A-B56. Remarkably, new mechanisms that modulate regulator and substrate binding continue to be discovered. For example, we recently discovered that dynamic charge-charge interactions modulate the affinities of PPP-specific SLiMs for their cognate PPPs. We also discovered that similar dynamic electrostatic interactions can, in some cases, actively direct substrate specificity. Most recently, we have discovered members of this family engage regulators and substrates using SHelMs (short helical motifs) in addition to SLiMs. Finally, we have also shown that SLiM phosphorylation has opposing effects on PPP binding, leading to differential PPP recruitment to the same substrate in distinct cellular states. Here, we will present new data illustrating some of the diverse and novel mechanisms used by regulators and substrates to engage their cognate PPPs and, in turn, direct PPP holoenzyme formation and activity. We will also include our most recent work on the tyrosine phosphatase SHP2.=0D=0A=
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More information about Prof. Page and her research: https://sites.google.com/view/pagelaboratory/home 
LOCATION:Perrin LT (Blizard, Whitechapel campus)
DTSTART:20261112T130000
DTEND:20261112T140000
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