Yossef Baidi
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Yossef Baidi has a total of 32 co-authors. Here are the top co-authors by number of shared publications:
- Adam Skepner
Broad Institute
1 shared publication - Alessandra Ianari
Cancer Program, The Broad Institute of MIT and Harvard, 415 Main Street, Cambridge MA 02142
1 shared publication - Alissa J Nelson
Cell Signaling Technology
1 shared publication Annabel K. Sangree
Genetic Perturbation Platform, Broad Institute, Cambridge, MA 02142, USA
1 shared publicationAudrey Griffith
Genetic Perturbation Platform, Broad Institute, Cambridge, MA 02142, USA
1 shared publication- Brian J. McMillan
Jnana Therapeutics (United States), United States
1 shared publication
Latest Publications
- Open Access
Molecular basis for substrate recruitment to the PRMT5 methylosome
PRMT5 is an arginine methyltransferase and a therapeutic target in MTAP null cancers. PRMT5 utilizes adaptor proteins for substrate recruitment through a previously undefined mechanism. Here, we identify an evolutionarily conserved peptide sequence shared among the three known substrate adaptors (pICln/CLNS1A, RIOK1 and COPR5) and show it is necessary and sufficient for interaction with PRMT5. We structurally resolve the interface with PRMT5 and show via genetic perturbation that it is required for methylation of adaptor-recruited substrates including the spliceosome, histones, and ribosome assembly complexes. Genetic disruption of the PRMT5-substrate adaptor interface leads to a hypomorphic decrease in growth of MTAP null tumor cells and is thus a novel site for development of therapeutic inhibitors of PRMT5.
Open AccessMolecular basis for substrate recruitment to the PRMT5 methylosome
PRMT5 is an arginine methyltransferase and a therapeutic target in MTAP null cancers. PRMT5 utilizes adaptor proteins for substrate recruitment through a previously undefined mechanism. Here, we identify an evolutionarily conserved peptide sequence shared among the three known substrate adaptors (pICln/CLNS1A, RIOK1 and COPR5) and show it is necessary and sufficient for interaction with PRMT5. We structurally resolve the interface with PRMT5 and show via genetic perturbation that it is required for methylation of adaptor-recruited substrates including the spliceosome, histones, and ribosome assembly complexes. Genetic disruption of the PRMT5-substrate adaptor interface leads to a hypomorphic decrease in growth of MTAP null tumor cells and is thus a novel site for development of therapeutic inhibitors of PRMT5.