Abstract:
:Pladienolide, herboxidiene and spliceostatin have been identified as splicing modulators that target SF3B1 in the SF3b subcomplex. Here we report that PHF5A, another component of this subcomplex, is also targeted by these compounds. Mutations in PHF5A-Y36, SF3B1-K1071, SF3B1-R1074 and SF3B1-V1078 confer resistance to these modulators, suggesting a common interaction site. RNA-seq analysis reveals that PHF5A-Y36C has minimal effect on basal splicing but inhibits the global action of splicing modulators. Moreover, PHF5A-Y36C alters splicing modulator-induced intron-retention/exon-skipping profile, which correlates with the differential GC content between adjacent introns and exons. We determine the crystal structure of human PHF5A demonstrating that Y36 is located on a highly conserved surface. Analysis of the cryo-EM spliceosome Bact complex shows that the resistance mutations cluster in a pocket surrounding the branch point adenosine, suggesting a competitive mode of action. Collectively, we propose that PHF5A-SF3B1 forms a central node for binding to these splicing modulators.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Teng T,Tsai JH,Puyang X,Seiler M,Peng S,Prajapati S,Aird D,Buonamici S,Caleb B,Chan B,Corson L,Feala J,Fekkes P,Gerard B,Karr C,Korpal M,Liu X,T Lowe J,Mizui Y,Palacino J,Park E,Smith PG,Subramanian V,Wu ZJdoi
10.1038/ncomms15522subject
Has Abstractpub_date
2017-05-25 00:00:00pages
15522issn
2041-1723pii
ncomms15522journal_volume
8pub_type
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