Shahar Sukenik
Syracuse University, NY·Biophysics
Most human proteins contain stretches that never settle into a single fixed shape. These intrinsically disordered regions (IDRs), found in over 70% of human proteins, instead constantly switch between many shapes.
- Fields
Biophysics
Biochemistry
Chemistry
- Topics
intrinsically disordered proteins
intrinsically disordered regions
structural ensembles
- Grants
- 1 known grant, through Dec 2030
What they work on
- Determine when the structural preferences of disordered regions in transcription factors affect their function, by linking ensemble structure to transcriptional activity in live cells.
- Test whether disease-linked single-point missense mutations, single amino acid changes, alter the structural ensemble and gene-activating function of transcription factor disordered regions.
- Test whether a stressed cellular environment shifts the structural preferences of transcription factor disordered regions and changes their ability to drive gene expression in live cells.
More about the research
That shifting collection of shapes is called an ensemble. A growing idea in the field is that an ensemble's structural preferences, meaning which shapes it favors, help decide what the protein does. How this works is still largely unknown. It matters because these preferences can shift when a protein's sequence changes or when the inside of the cell changes, for example under stress.
Why it matters
Transcription factors control which genes are switched on, and their disordered regions help recruit the cell's gene-reading machinery. Learning how mutations and cellular stress reshape these regions could explain how gene regulation goes wrong in disease. That understanding could, in turn, show how single disease-linked mutations disrupt transcription factor function.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Katerina Cermakova
Baylor College of Medicine, TX·Biochemistry
Determine how chromatin and transcription state influence RNA export of highly transcribed genes, by rapidly manipulating the IDR-domain interaction in living cells and measuring nascent RNA and genomic outcomes.
Thomas Martinez
University of California-Irvine, CA·Biochemistry
Select curated sets of disordered microproteins whose short linear motifs (SLiMs) match those in proteins for signaling, RNA metabolism or cell organization, to predict likely functions.
Beat Vogeli
University of Colorado Denver/Anschutz Medical Campus, CO·Biophysics
Determine how the dynein light intermediate chain (LIC), a flexible disordered region, works with cargo-specific adaptor proteins and phosphorylation to let a single cytoplasmic dynein carry many different cargoes, using NMR and other biophysical methods.
The school
Syracuse University: 13 labs on PI Pages, $199M a year on research, 168 research doctorates a year.
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