Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

Serine Phosphorylation of SR Proteins Is Required for Their Recruitment to Sites of Transcription in vivo

Tom Misteli, Javier F. Cáceres, Jade Q. Clement, Adrian R. Krainer, Miles F. Wilkinson and David L. Spector
The Journal of Cell Biology
Vol. 143, No. 2 (Oct. 19, 1998), pp. 297-307
Stable URL: http://www.jstor.org/stable/1618836
Page Count: 11
  • More info
  • Cite this Item
Serine Phosphorylation of SR Proteins Is Required for Their Recruitment to Sites of Transcription in vivo
Preview not available

Abstract

Expression of most RNA polymerase II transcripts requires the coordinated execution of transcription, splicing, and 3′ processing. We have previously shown that upon transcriptional activation of a gene in vivo, pre-mRNA splicing factors are recruited from nuclear speckles, in which they are concentrated, to sites of transcription (Misteli, T., J.F. Cáceres, and D.L. Spector. 1997. Nature. 387:523-527). This recruitment process appears to spatially coordinate transcription and pre-mRNA splicing within the cell nucleus. Here we have investigated the molecular basis for recruitment by analyzing the recruitment properties of mutant splicing factors. We show that multiple protein domains are required for efficient recruitment of SR proteins from nuclear speckles to nascent RNA. The two types of modular domains found in the splicing factor SF2/ASF exert distinct functions in this process. In living cells, the RS domain functions in the dissociation of the protein from speckles, and phosphorylation of serine residues in the RS domain is a prerequisite for this event. The RNA binding domains play a role in the association of splicing factors with the target RNA. These observations identify a novel in vivo role for the RS domain of SR proteins and suggest a model in which protein phosphorylation is instrumental for the recruitment of these proteins to active sites of transcription in vivo.

Page Thumbnails

  • Thumbnail: Page 
297
    297
  • Thumbnail: Page 
298
    298
  • Thumbnail: Page 
299
    299
  • Thumbnail: Page 
300
    300
  • Thumbnail: Page 
301
    301
  • Thumbnail: Page 
302
    302
  • Thumbnail: Page 
303
    303
  • Thumbnail: Page 
304
    304
  • Thumbnail: Page 
305
    305
  • Thumbnail: Page 
306
    306
  • Thumbnail: Page 
307
    307