BioRxiv: Intrinsically disordered SERBP1 regulates translation through topology-driven G-quadruplex recognition (Libich Lab)

March 19, 2026

      Antoine Baudin, Hoang H. Dinh, Kira Breunig, Xuifen Lei, Xiaoping Xu, View Luiz O. Penalva, David S. Libich Abstract Serpine mRNA-binding protein 1 (SERBP1) is an intrinsically disordered RNA-binding protein that regulates translation and ribosome biogenesis through interactions with ribosomes and other molecular complexes. Despite its regulatory importance and implication in cancer [...]

Protein Science: Molecular basis of EWS interdomain self-association and its role in condensate formation (Libich Lab)

September 22, 2025

Erich J. Sohn, Kandarp A. Sojitra, Leticia Rodrigues, Xiaoping Xu, Bess Frost, Jeetain Mittal, David S. Libich Abstract Ewing sarcoma, the second most common pediatric bone and soft tissue cancer, is caused by the aberrant fusion of the RNA-binding protein EWS (EWS) low-complexity domain (EWSLCD) to the DNA-binding domain of the transcription factor friend leukemia integration 1 (FLI1). The resulting fusion, [...]

Biochemistry: The Spliceosomal Peptidyl Prolyl Isomerase Like 1 Interacts with the Low-Complexity Domain of the RNA Binding Protein EWS Modulating Its Phase Separation Behavior (Libich Lab)

August 8, 2025

George L Parra 1, Erich J Sohn 1, Xiaoping Xu 1, David S Libich 1 Abstract RNA-binding protein EWS, a member of the FET (FUS, EWS, TAF15) family, contributes to mRNA biogenesis through roles in transcription, splicing, and RNA transport. Despite evidence linking EWS to spliceosomal complexes, its interactions with spliceosome-associated cyclophilins remain unclear. Here, we describe the first structural and biochemical [...]

Biochemistry: The Spliceosomal Peptidyl Prolyl Isomerase Like 1 Interacts with the Low-Complexity Domain of the RNA Binding Protein EWS Modulating Its Phase Separation Behavior (Libich Lab)

July 17, 2025

Abstract RNA binding protein EWS, a member of the FET (FUS, EWS, TAF15) family, contributes to mRNA biogenesis through roles in transcription, splicing, and RNA transport. Despite evidence linking EWS to spliceosomal complexes, its interactions with spliceosome-associated cyclophilins remain unclear. Here, we describe the first structural and biochemical characterization of the EWS low-complexity domain (EWSLCD) [...]

BioMolecular NMR Assignments: The 1H, 15N and 13C backbone resonance assignments of the N-terminal (1-149) domain of Serpine mRNA Binding Protein 1 (SERBP1) (Libich Lab)

May 30, 2025

Antoine Baudin, Hoang H. Dinh, Xiaoping Xu & David S. Libich Abstract Serpine mRNA-Binding Protein 1 (SERBP1) is an RNA-binding protein implicated in diverse cellular functions, including translational regulation, tumor progression, and stress response. It interacts with ribosomal subunits, RNA, and proteins involved in stress granules, contributing to processes such as phase separation and epigenetic regulation. [...]


PNAS: Phase separation of the oncogenic fusion protein EWS::FLI1 is modulated by its DNA-binding domain (Libich & Bishop Labs)

May 16, 2025

Emily E. Selig  Erich J. Sohn  Aiola Stoja, Alma K. Moreno-Romero, Shivani Akula, Xiaoping Xu, Alexander J. R. Bishop, and David S. Libich Significance The oncogenic fusion protein, EWS::FLI1, responsible for more than 85% of Ewing sarcoma tumors, combines the transactivation domain from EWS and the DNA-binding domain (DBD) from Friend leukemia integration 1 (FLI1). The fusion impacts the function of wild-type EWS and drives oncogenesis via [...]

Cell Reports: Distinct roles of the two BRCA2 DNA-binding domains in DNA damage repair and replication fork preservation (Sung, Libich Labs)

May 7, 2025

Francisco E. Neal1,2 ∙ Wenjing Li1 ∙ Mollie E. Uhrig3,4 ∙ Jeffrey N. Katz1,2 ∙ Shahrez Syed1,2 ∙ Neelam Sharma3 ∙ Arijit Dutta1,2,8 ∙ Sandeep Burma1,5 ∙ Robert Hromas6 ∙ Alexander V. Mazin1 ∙ Eloise Dray1 ∙ David S. Libich1,2 ∙ Shaun K. Olsen1,2 ∙ Elizabeth V. Wasmuth1,2 ∙ Weixing Zhao1,2 ∙ Claus S. Sørensen7 Highlights BRCA2 OB-fold DNA-binding domain has specificity for ssDNA BRCA2 C-terminal DNA-binding domain has specificity for dsDNA OB-fold DNA-binding domain is needed for DNA repair and replication fork protection C-terminal DNA-binding domain functions primarily in replication fork protection Summary Homologous recombination (HR) removes DNA double-strand breaks [...]

Biomolecular NMR Assignments: The 1H, 15N and 13C backbone resonance assignments of the N-terminal (1-149) domain of Serpine mRNA Binding Protein 1 (SERBP1) (Libich Lab)

March 31, 2025

Antoine Baudin1, Hoang H Dinh1, Xiaoping Xu1, David S Libich2 Abstract Serpine mRNA-Binding Protein 1 (SERBP1) is an RNA-binding protein implicated in diverse cellular functions, including translational regulation, tumor progression, and stress response. It interacts with ribosomal subunits, RNA, and proteins involved in stress granules, contributing to processes such as phase separation and epigenetic regulation. Recent studies have [...]

ELife: SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis (Libich, Penalva, et al)

February 13, 2025

Kira Breunig#1, Xuifen Lei#1, Mauro Montalbano#23, Gabriela D A Guardia4, Shiva Ostadrahimi15, Victoria Alers156, Adam Kosti15, Jennifer Chiou7, Nicole Klein1, Corina Vinarov1, Lily Wang1, Mujia Li1, Weidan Song8, W Lee Kraus8, David S Libich16, Stefano Tiziani7910, Susan T Weintraub6, Pedro A F Galante4, Luiz O Penalva15 Abstract RNA binding proteins (RBPs) containing intrinsically disordered regions (IDRs) are present in diverse molecular complexes where they function as dynamic regulators. Their characteristics promote liquid-liquid phase [...]