TREX, SR proteins and export of mRNA.
The machineries involved in gene expression are highly conserved from yeast to metazoans. However, a fundamental difference between these organisms is that most yeast genes lack introns whereas the converse is true in higher organisms. Recent studies of the TREX complex, which functions in mRNA export, unexpectedly revealed that this complex is recruited by the transcription machinery in yeast whereas the TREX complex appears to be recruited by the splicing machinery in mammals. Studies during the past year also revealed a possible conserved role for SR protein dephosphorylation in regulating the interaction between SR proteins and the mRNA export receptor TAP (Mex67 in yeast). There is also an interesting possibility that an SR protein-TREX complex interaction is a conserved part of the mRNA export machinery.
Reed
Robin
R
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA. rreed@hms.harvard.edu
Cheng
Hong
H
D021581:Active Transport, Cell Nucleus / Q000502:physiology; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D006801:Humans; D007438:Introns / Q000235:genetics; D008954:Models, Biological; D046912:Multiprotein Complexes / Q000502:physiology*; D009687:Nuclear Proteins / Q000502:physiology*; D010750:Phosphoproteins; D012326:RNA Splicing / Q000502:physiology; D034443:RNA Transport / Q000502:physiology; D012333:RNA, Messenger / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000502:physiology*; D000068103:Serine-Arginine Splicing Factors; D015003:Yeasts / Q000235:genetics / Q000378:metabolism
D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D010750:Phosphoproteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D000068103:Serine-Arginine Splicing Factors