RioK1 a new interactor of protein arginine methyltransferase 5 (PRMT5) competes with pICln for binding and modulates PRMT5 complex composition and substrate specificity.
Lsm10 and Lsm11 which replace the Sm proteins D1 and D2 in the histone RNA processing U7 snRNPs associate with pICln in vitro and in vivo without receiving sDMA modifications and with PRMT5 and SMN complexes
Data show that ICln159 a truncated ICln mutant belongs to the pleckstrin homology (PH) domain family of proteins and interacts with LSm4 a protein involved in splicing and mRNA degradation.
revealed an increase of ICln in the mesothelioma cell membrane under hypotonic conditions an event possibly related to the activation of Cl(-) channels
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