Table 1 (continued)
PRMT
Type
Substrates
Function/disease relation
Effect by inhibition
(auto)
Splicing factors
RNA-binding
proteins
Transcription
factors
Coactivators
PRMT5
Type II
Histone H2A
Arg3
Histone H3
Arg8
Histone H4
Arg3
Sm proteins
Ribosomal
proteins
Nuclear factors
Transcription
factors
Tumour
suppressors
Involved in embryogenesis and
gene transcription
Binding partners regulate activity and substrate specificity
Upregulated in breast, colorectal, lung, epithelial ovarian cancer, lymphomas and melanoma
Antiproliferative in MCL cells and
MCL mice. Phase I clinical trials on
solid tumours and non-Hodgkin’s
lymphoma
PRMT6
Type I
Histone H2A
Arg3
Histone H2A
Arg29
Histone H3
Arg2
Histone H3
Arg8
Histone H3
Arg42
Histone H4
Arg3
Chromatin
proteins
DNA-binding
proteins
PRMT6
(auto)
Viral proteins
Overexpressed in bladder, lung
and prostate cancer
Downregulated in melanoma
Associated with pulmonary disorders
Reduces HIV-1 production and
viral replication
Dose-dependent decrease in H3R2
methylation in A375 cells
PRMT7
Type
III
RxR motif
Histone H2A
Arg3
Histone H2B
Arg29
Histone H2B
Arg31
Histone H2B
Arg33
Histone H4
Arg3
Histone H4
Arg17
Histone H4
Arg19
Sm proteins
Linked to breast cancer metastasis, DNA damage and parasite
infection
Increases tumour sensitivity to
chemotherapeutics
Unknown
(continued)
PRMT Inhibitors
187