Disease relevance of SNRPD3

• Examination of PRMT7 expressed in E. coli demonstrated that peptides corresponding to sequences contained in histone H4, myelin basic protein, and SmD3 were methylated [1].
• Improved serological differentiation between systemic lupus erythematosus and mixed connective tissue disease by use of an SmD3 peptide-based immunoassay [2].

High impact information on SNRPD3

• We show that SMN binds preferentially to the dimethylarginine-modified RG domains of SmD1 and SmD3 [3].
• Gemin3 interacts directly with SMN, as well as with SmB, SmD2, and SmD3 [4].
• SMN binds preferentially and directly to the symmetrical dimethylarginine (sDMA)-modified arginine- and glycine-rich (RG-rich) domains of SmD1 and SmD3 [5].
• The symmetrical dimethylarginine post-translational modification of the SmD3 protein is not required for snRNP assembly and nuclear transport [6].
• We show that the elimination of this methylation in the SmD3 protein, by mutating the modified arginines to leucines, does not interfere with the assembly and the nuclear transport of the transiently expressed SmD3 variant [6].

Biological context of SNRPD3

• The SmB, SmD1, and SmD3 proteins have the rare symmetrical dimethylarginine post-translational modification in their C-termini [6].

Other interactions of SNRPD3

• JBP1 binds SmD1 and SmD3 via their RG domains, while pICln binds the Sm domains [5].

References