[3dem] Free CryoEM Webinar - June 26th, 2025 12pm (Eastern)

[Kjirsten Wheeler]

Hello Interested Researchers,

Just a final reminder that our upcoming NIH sponsored Joint CryoEM Service Centers Webinar Series "Decoding mechanisms that control PPP specificity" by Dr. Rebecca Page on June 26th, at 12pm (Eastern Time) (see attachment or below for details).

Registration is at no-cost, but sign-up is required: https://urldefense.com/v3/__https://us02web.zoom.us/webinar/register/WN_ZbHoCTb6SCe7zhCKb8uMvA__;!!Mih3wA!Cppzb987WvTl2maEVSMPlJ4clRbhB2Hi8qyWyMRAOg9fE90OZJh5hJ2_0TxwGe6nvyIKYjlyoTziypBgOTIw$ 

For more information regarding the National CryoEM Service Centers can be found at https://urldefense.com/v3/__https://www.cryoemcenters.org/cryoem-centers/__;!!Mih3wA!Cppzb987WvTl2maEVSMPlJ4clRbhB2Hi8qyWyMRAOg9fE90OZJh5hJ2_0TxwGe6nvyIKYjlyoTziysHiPtXP$ .

Best,
_________________________
Kjirsten Wheeler
PNCC Administrative Coordinator
Pacific Northwest Cryo-EM Center
a PNNL and OHSU affiliation    Website<https://urldefense.com/v3/__https:/pncc.labworks.org/__;!!Mi0JBg!burdB2N3-jSi-4APwohcbkMgXzrhpmrr-Q_XadX2I6g6qfUKLs-MOS_CSrl8z8tr$>   PNCC Twitter<https://urldefense.com/v3/__https:/twitter.com/CryoEM_PNCC__;!!Mi0JBg!burdB2N3-jSi-4APwohcbkMgXzrhpmrr-Q_XadX2I6g6qfUKLs-MOS_CSvMnTGN3$>  LinkedIn<https://urldefense.com/v3/__https://ohsuitg.sharepoint.com/sites/PROJ.PNCC/Shared*20Documents/General/PNCC_Workshops*20&*20Training/SerialEM*20Screening*20Workshop/pacific-northwest-cryo-em-center__;JSUlJSU!!Mih3wA!Cppzb987WvTl2maEVSMPlJ4clRbhB2Hi8qyWyMRAOg9fE90OZJh5hJ2_0TxwGe6nvyIKYjlyoTziyk14U30l$ >
wheelekj at ohsu.edu<mailto:wheelekj at ohsu.edu>


_______________________________

CryoEM Current Practices Webinar


Decoding mechanisms that control PPP specificity

[cid:image001.jpg at 01DBD0BF.504742E0]


Rebecca Page, Ph.D.
Professor of Cellular Biology
Cell Biology, University of Connecticut Health

12PM EDT / 9AM PDT Thursday, June 26th, 2025

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 also 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.  Here, we present recent data, based on cryo-EM structures of PP2A:B55 bound to inhibitors, substrates and regulators, that illustrate the diverse and novel mechanisms used by regulators and substrates to engage their cognate PPPs and, in turn, direct PPP holoenzyme formation and activity.

All are welcome to attend. Registration is at no-cost, but sign-up is required:
https://urldefense.com/v3/__https://us02web.zoom.us/webinar/register/WN_ZbHoCTb6SCe7zhCKb8uMvA__;!!Mih3wA!Cppzb987WvTl2maEVSMPlJ4clRbhB2Hi8qyWyMRAOg9fE90OZJh5hJ2_0TxwGe6nvyIKYjlyoTziypBgOTIw$ 


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