Y
Yuan Lin
Researcher at University of Texas Southwestern Medical Center
Publications - 6
Citations - 2812
Yuan Lin is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: RNA & Protein domain. The author has an hindex of 5, co-authored 6 publications receiving 2027 citations. Previous affiliations of Yuan Lin include Howard Hughes Medical Institute.
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Journal ArticleDOI
Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
Yuan Lin,David S.W. Protter,Michael K. Rosen,Michael K. Rosen,Michael K. Rosen,Roy Parker,Roy Parker,Roy Parker +7 more
TL;DR: It is demonstrated that the disordered regions of key RNP granule components and the full-length granule protein hnRNPA1 can phase separate in vitro, producing dynamic liquid droplets.
Journal ArticleDOI
Compositional Control of Phase-Separated Cellular Bodies
Salman F. Banani,Allyson M. Rice,William B. Peeples,Yuan Lin,Saumya Jain,Roy Parker,Michael K. Rosen +6 more
TL;DR: The data suggest a conceptual framework for considering the composition and control of cellular bodies assembled through heterotypic multivalent interactions, suggesting how their compositions could be controlled by levels of PML SUMOylation or cellular mRNA concentration, respectively.
Journal ArticleDOI
Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs
TL;DR: Results show that low-complexity IDRs can modulate LLPS both positively and negatively, depending on the degree of aromaticity and phosphorylation status, and provide plausible mechanisms by which these sequences could alter RNA granule properties on evolutionary and cellular timescales.
Journal ArticleDOI
Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly.
David S.W. Protter,Bhalchandra S. Rao,Briana Van Treeck,Yuan Lin,Laura S. Mizoue,Michael K. Rosen,Roy Parker +6 more
TL;DR: Evidence is provided for an assembly mechanism of large cellular structures wherein specific protein-protein or protein-RNA interactions act together with promiscuous interactions of intrinsically disordered regions (IDRs).
Journal ArticleDOI
Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites
Takuya Yoshizawa,Rustam Ali,Jenny Jiou,Ho Yee Joyce Fung,Kathleen A. Burke,Seung Joong Kim,Yuan Lin,Yuan Lin,William B. Peeples,William B. Peeples,Daniel J. Saltzberg,Michael M. Soniat,Jordan M. Baumhardt,Rudolf Oldenbourg,Andrej Sali,Nicolas L. Fawzi,Michael K. Rosen,Michael K. Rosen,Yuh Min Chook,Yuh Min Chook +19 more
TL;DR: A model where high-affinity binding of karyopherin-β2 to the FUS PY-NLS tethers the proteins together, allowing multiple, distributed weak intermolecular contacts to disrupt FUS self-association, blocking LLPS is proposed.