Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions.
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Intrinsically disordered regions (IDRs) of proteins are implicated in key macromolecular interactions. However, the molecular forces underlying IDR function within multicomponent assemblies remain elusive. By combining thermodynamic and structural data, we have discovered an allostery-based mechanism regulating the soluble core region of the nuclear pore complex (NPC) composed of nucleoporins Nup53, Nic96, and Nup157. We have identified distinct IDRs in Nup53 that are functionally coupled when binding to partner nucleoporins and karyopherins (Kaps) involved in NPC assembly and nucleocytoplasmic transport. We show that the Nup53·Kap121 complex forms an ensemble of structures that destabilize Nup53 hub interactions. Our study provides a molecular framework for understanding how disordered and folded domains communicate within macromolecular complexes.
SubjectScience & Technology
Science & Technology - Other Topics
Published Version (Please cite this version)10.1126/sciadv.aax1836
Publication InfoCoutavas, Elias; Blus, Bartlomiej Jan; Koh, Junseock; Krolak, Aleksandra; Seo, Hyuk-Soo; & Blobel, Günter (2019). Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions. Science advances, 5(11). pp. eaax1836. 10.1126/sciadv.aax1836. Retrieved from https://hdl.handle.net/10161/20158.
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Assistant Professor in Medicine
Dr. Coutavas was recruited to DUMC in 2020 by Dr. Patty Lee, Chief of the Division of Pulmonary, Allergy & Critical Care, as the Director of divisional science operations. He has a PhD in Cell and Molecular Biology from NYU and previously worked at the Rockefeller University with Günter Blobel, the 1999 recipient of the Nobel Prize in Physiology and Medicine. His scientific expertise is in biochemistry, molecular biology, and bioimaging, and he has extensive experience in