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VIDEO: Shahar Sukenik on Turning Protein Disorder into Function: Is the Solution the Solution?

On June 23, UC Merced’s Shahar Sukenik treated Dewpoint and to a fascinating Kitchen Table Talk on his lab’s work. Shahar has been studying the behaviors of proteins in cells since his PhD with Daniel Harries at the Hebrew University of Jerusalem and his postdoc with Martin Gruebele at Urbana-Champaign. In 2018 he opened his own lab at UC Merced to study the interaction between proteins and their surrounding environment both in vitro and in cells, with a special emphasis on the breakdown of homeostasis, which is relevant for many pathological conditions including cancer, viral infection, and other metabolically linked diseases. In this research, his lab deploys a wide range of methods such as live cell imaging, spectroscopy, and computational modeling.

In his talk, Shahar discussed how his lab identifies the hidden structures of IDRs and how these hidden structures alter the ability of proteins to form specific, functional, and stable condensates. We were all brimming with questions afterward, and Shahar kindly provided written answers to the ones he didn’t have time to answer during the talk. You can find those here, and the recording of his talk below.

Shahar Sukenik on Turning Protein Disorder into Function: Is the Solution the Solution?

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Mark Murcko (00:00:00):
Hi everybody. Good to see you all again. Yeah, it’s interesting because we’ve heard so many great comments about the whole lecture series, this whole idea of the Kitchen Table Talks for the whole community. We’re getting a lot of great feedback from people around the world about how they really enjoy these lectures, find them fun and educational and so we’re really glad to hear that. That’s why we’re doing this, we’re doing this because we think that the whole condensate community can benefit. We’re all wrestling with the same scientific challenges and so it’s good to be thinking about these things together with everyone.

Mark Murcko (00:00:34):
So today we have Shahar Sukenik. He’s from University of California at Merced. I’m really excited about having Shahar here. Got his PhD at the Hebrew University of Jerusalem, and then did a postdoc at Urbana-Champaign, really focusing on microscopy, really thinking carefully about the interactions of proteins in live cells. And obviously over the years has gotten attracted by the condensate bug, like all the rest of us. And three years ago took his faculty position at Merced where he is now an assistant professor.

Mark Murcko (00:01:19):
And really interesting work because it highlights the interactions between proteins and their environments, both in vitro and in vivo in a cellular context. And of course, Shahar does this with an amazing range of technologies, live cell imaging and spectroscopy, computational modeling, other things and so really applying a multi-disciplinary approach. And that’s a common theme, isn’t it? A lot of the condensate lectures we’ve heard really rely on such an interesting blend of technology to tackle these challenging problems. And so in particular, he’s been focused on homeostasis and we all know the critical nature of that and, and how the metabolic rewiring affects proteins in a variety of ways and how relevant that is for cancer and viral infection and lots of other pathology.

Mark Murcko (00:02:22):
And of course that leads to IDRs, which are such an essential part of this whole process. And so naturally a lot of the work that Shahar does is related to understanding the way the IDRs and the other aspects of proteins lead them to form these very specific and functional and stable condensates. And so, very exciting to have you here today and your title this morning is, Turning Protein Disorder into Function: Is the Solution the Solution? Floor is yours.

Shahar Sukenik (00:02:54):
Thanks so much, Mark. So first I’d just like to start by thanking Jill for this invite and Mark for that fantastic intro, which basically turns my intro obsolete, but I’m going to try doing it anyway. So it’s really great to be here this morning. And so I think we’ll just jump right into it. And the place I’d like to start with is a slight apology in that while there will be some discussion of condensates most of this talk, we’re going to zoom in and really focus not on the collective behavior of proteins, but rather on the behavior of the monomer. And like Mark said before, to understand the collective behavior of these molecules, it’s really important to first form a good understanding of how they behave when they’re on their own. So that’s kind of our entry point…


Question from Gaurav Chauhan: Could the sequence-dependent changes (in IDPs, not in GS homopolymer) in persistence length affect the values of R_e one would get from FRET experiments?
Shahar’s Response: So this was exactly the concern that made us decide to correlate FRET and SAXS. We hypothesized that the changes won’t be only from distance, but also for example from preferred orientation of the dipole transition moment in the fluorescent proteins. However, this type of orientation is only possible when the sequence is non-isotropic – in other words, when the sequence has some structure to it. The fact that our experiments corroborated this effect is further evidence of hidden structure…

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