scholarly journals Identification of the Rigid Core for Aged Liquid Droplets of an RNA-Binding Protein Low Complexity Domain

2021 ◽  
Author(s):  
Blake D. Fonda ◽  
Khaled M. Jami ◽  
Natalie R. Boulos ◽  
Dylan T. Murray
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Low Complexity ◽  
Liquid Droplets ◽  
Rigid Core

scholarly journals The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β cores

2021 ◽  
Vol 118 (42) ◽  
pp. e2114412118
Author(s):  
Masato Kato ◽  
Steven L. McKnight
Keyword(s):  
Phase Separation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Low Complexity ◽  
Terminal Region ◽  
Aqueous Environment ◽  
Fused In Sarcoma ◽  
Biochemical Assays ◽  
Biologic Function

The low-complexity (LC) domain of the fused in sarcoma (FUS) RNA binding protein self-associates in a manner causing phase separation from an aqueous environment. Incubation of the FUS LC domain under physiologically normal conditions of salt and pH leads to rapid formation of liquid-like droplets that mature into a gel-like state. Both examples of phase separation have enabled reductionist biochemical assays allowing discovery of an N-terminal region of 57 residues that assembles into a labile, cross-β structure. Here we provide evidence of a nonoverlapping, C-terminal region of the FUS LC domain that also forms specific cross-β interactions. We propose that biologic function of the FUS LC domain may operate via the mutually exclusive use of these N- and C-terminal cross-β cores. Neurodegenerative disease–causing mutations in the FUS LC domain are shown to imbalance the two cross-β cores, offering an unanticipated concept of LC domain function and dysfunction.

O-Linked-N-Acetylglucosaminylation of the RNA-Binding Protein EWS N-Terminal Low Complexity Region Reduces Phase Separation and Enhances Condensate Dynamics

2021 ◽  
Author(s):  
Michael L. Nosella ◽  
Maria Tereshchenko ◽  
Iva Pritišanac ◽  
P. Andrew Chong ◽  
Jeffrey A. Toretsky ◽  
...  
Keyword(s):  
Phase Separation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Low Complexity

scholarly journals N‐terminal acetylation modestly enhances phase separation and reduces aggregation of the low‐complexity domain of RNA ‐binding protein FUS

2021 ◽  
Author(s):  
Anna S. Bock ◽  
Anastasia C. Murthy ◽  
Wai Shing Tang ◽  
Nina Jovic ◽  
Frank Shewmaker ◽  
...  
Keyword(s):  
Phase Separation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Low Complexity

235: The RNA-Binding Protein IMP3: A Novel Molecular Marker Predicts Progression of Superficial (TA and T1) Urothelial Carcinomas of Bladder

2007 ◽  
Vol 177 (4S) ◽  
pp. 78-79
Author(s):  
Lioudmila Sitnikova ◽  
Gary Mendese ◽  
Qin Lui ◽  
Bruce A. Woda ◽  
Di Lu ◽  
...  
Keyword(s):  
Molecular Marker ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Urothelial Carcinomas

Author response for "Inhibition of osteoclastogenesis by the RNA‐binding protein QKI5: a novel approach to protect from bone resorption"

2019 ◽  
Author(s):  
Benjamin Rauwel ◽  
Yannick Degboe ◽  
Katy Diallo ◽  
Souraya Sayegh ◽  
Michel Baron ◽  
...  
Keyword(s):  
Bone Resorption ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Author Response ◽  
Novel Approach

The RNA-binding protein Musashi-2 (MSI2) controls mRNA processing and translational regulation via interactions with SFPQ and PIWIL1 during mammalian spermatogenesis

2014 ◽  
Author(s):  
Jessie M Sutherland ◽  
Alexander P Sobinoff ◽  
Kate Redgrove ◽  
Tara-Lynne Davidson ◽  
Nicole A Siddall ◽  
...  
Keyword(s):  
Translational Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Mrna Processing
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