Disease relevance of Khsrp

• In normally cultured neuroblastoma cells, these src RNA foci contain PTB, but little KSRP [1].
• Human KHSRP is a positional candidate gene for familial febrile convulsion and Cayman type cerebellar ataxia [2].

High impact information on Khsrp

• KSRP phosphorylated by p38 displays compromised binding to ARE-containing transcripts and fails to promote their rapid decay, although it retains the ability to interact with the mRNA degradation machinery [3].
• p38-dependent phosphorylation of the mRNA decay-promoting factor KSRP controls the stability of select myogenic transcripts [3].
• Colocalization experiments of KSRP with PTB in a mouse neuroblastoma cell line determined that both proteins are present in the perinucleolar compartment (PNC), as well as in other nuclear enrichments [1].
• In contrast, HeLa cells do not show prominent KSRP staining in the PNC, even though PTB labeling identified the PNC in these cells [1].
• In this study, we mapped the gene (gene symbols KHSRP and Khsrp) to human chromosome 19 by using radiation hybrid panels and to mouse chromosome 17 by studying an interspecific backcross panel [2].

Biological context of Khsrp

• The K homology-type splicing regulatory protein, KSRP, activates splicing through intronic splicing enhancer sequences [2].
• Comparative analysis of the human and mouse genomes indicates that the KHSRP gene is located in regions of conserved synteny between the two species [2].

Regulatory relationships of Khsrp

• Our results uncover an unanticipated role for KSRP in establishing a biochemical link between differentiation-activated p38 signaling and turnover of myogenic mRNAs [3].

Other interactions of Khsrp

• Overexpression of KSRP selectively impairs induction of ARE-containing early myogenic transcripts, without affecting p38-mediated transcriptional responses [3].

References