Ontology highlight
ABSTRACT:
SUBMITTER: Mulvaney KM
PROVIDER: S-EPMC9016627 | biostudies-literature | 2021 Sep
REPOSITORIES: biostudies-literature
Mulvaney Kathleen M KM Blomquist Christa C Acharya Nischal N Li Ruitong R Ranaghan Matthew J MJ O'Keefe Meghan M Rodriguez Diego J DJ Young Michael J MJ Kesar Devishi D Pal Debjani D Stokes Matthew M Nelson Alissa J AJ Jain Sidharth S SS Yang Annan A Mullin-Bernstein Zachary Z Columbus Josie J Bozal Fazli K FK Skepner Adam A Raymond Donald D LaRussa Salvatore S McKinney David C DC Freyzon Yelena Y Baidi Yossef Y Porter Dale D Aguirre Andrew J AJ Ianari Alessandra A McMillan Brian B Sellers William R WR
Molecular cell 20210805 17
PRMT5 is an essential arginine methyltransferase and a therapeutic target in MTAP-null cancers. PRMT5 uses 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 (CLNS1A, RIOK1, and COPR5) and show that it is necessary and sufficient for interaction with PRMT5. We demonstrate that PRMT5 uses modular adaptor proteins containing a common binding motif for sub ...[more]