Abstract:
:The human splicing factor 2, also called human alternative splicing factor (hASF), is the prototype of the highly conserved SR protein family involved in constitutive and regulated splicing of metazoan mRNA precursors. Here we report that the Drosophila homologue of hASF (dASF) lacks eight repeating arginine-serine dipeptides at its carboxyl-terminal region (RS domain), previously shown to be important for both localization and splicing activity of hASF. While this difference has no effect on dASF localization, it impedes its capacity to shuttle between the nucleus and cytoplasm and abolishes its phosphorylation by SR protein kinase 1 (SRPK1). dASF also has an altered splicing activity. While being competent for the regulation of 5' alternative splice site choice and activation of specific splicing enhancers, dASF fails to complement S100-cytoplasmic splicing-deficient extracts. Moreover, targeted overexpression of dASF in transgenic flies leads to higher deleterious developmental defects than hASF overexpression, supporting the notion that the distinctive structural features at the RS domain between the two proteins are likely to be functionally relevant in vivo.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Allemand E,Gattoni R,Bourbon HM,Stevenin J,Cáceres JF,Soret J,Tazi Jdoi
10.1128/MCB.21.4.1345-1359.2001subject
Has Abstractpub_date
2001-02-01 00:00:00pages
1345-59issue
4eissn
0270-7306issn
1098-5549journal_volume
21pub_type
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