Different requirements of the kinase and UHM domains of KIS for its nuclear localization and binding to splicing factors.
作者： Valérie Manceau , Clara L. Kielkopf , André Sobel , Alexandre Maucuer
DOI: 10.1016/J.JMB.2008.06.026
关键词:
摘要: Abstract The protein kinase KIS is made by the juxtaposition of a unique domain and C-terminal with U2AF homology motif (UHM), sequence for interaction initially identified in heterodimeric pre-mRNA splicing factor U2AF. This closely related to UHM large subunit, U2AF65. phosphorylates SF1, which turn enhances SF1 binding U2AF65 3′ splice site, an event known take place at early step spliceosome assembly. Here, analysis subcellular localization mutated forms indicates that necessary its nuclear localization. As case U2AF65, UHM-containing required factors SF3b155. efficiency SF3b155 similar pull-down assays. These results further support functional link factors. Interestingly, when compared other proteins, presents different specificity docking sites are present N-terminal region SF3b155, thus providing new insight into variety interactions mediated domains.
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