High impact information on Khdrbs3

• SLM-2 is an RNA-binding protein that is not tyrosine phosphorylated by Src or p59(fyn) [1].
• Together, our data suggest that Slm1 and Slm2 define a molecular link between phosphoinositide and sphingolipid signaling and thereby regulate actin cytoskeleton organization [2].
• SIAH1 targets the alternative splicing factor T-STAR for degradation by the proteasome [3].
• In mouse, T-STAR is co-expressed with SIAH1 during meiosis but, in humans, T-STAR is only strongly expressed after meiosis [3].
• Using a minigene transfection assay for alternative splicing activity we showed that human T-STAR, like its rodent orthologues can influence splice site choice and that human, but not mouse, T-STAR-dependent alternative splicing is modulated by SIAH1 [3].

Biological context of Khdrbs3

• The phosphorylation of SLM-1 and SLM-2 has functional relevance and leads to inhibition of their RNA-binding abilities [4].
• T-STAR is one of three members of the SAM68 family of RNA-binding proteins that have been shown to be involved in various gene expression pathways including the control of pre-mRNA splicing [3].
• It mapped to chromosome 15, while T-STAR mapped to the syntenic region on human chromosome 8 [5].
• Collectively these data suggest that SIAH-mediated down regulation of alternative splicing may be an important developmental difference between otherwise highly conserved T-STAR proteins [3].
• Our results suggest that Salp may function as a negative regulator of cell growth [6].

Anatomical context of Khdrbs3

• These findings demonstrate that the GSG domain is involved in protein localization and define a new compartment for Sam68, SLM-1, and SLM-2 in cancer cell lines [7].

Analytical, diagnostic and therapeutic context of Khdrbs3

• Comparative sequence analysis showed SIAH-mediated proteasomal degradation of T-STAR has evolved in the primate lineage [3].

References