A molecular link between SR protein dephosphorylation and mRNA export.
Proc Natl Acad Sci U S A
; 101(26): 9666-70, 2004 Jun 29.
Article
en En
| MEDLINE
| ID: mdl-15210956
ABSTRACT
In metazoans, multiple RNA-binding proteins, including the shuttling serine/arginine-rich (SR)-splicing factors, function as adapters for mRNA nuclear export by interacting with the export receptor TAP/nuclear export factor 1 (NXF1). Yet, it is unclear how interactions between adapters and TAP are regulated. Here, we demonstrate that the SR proteins 9G8 and ASF/SF2 exhibit higher affinity for TAP/NXF1 when hypophosphorylated. 9G8 is recruited to the pre-mRNA in a hyperphosphorylated form but becomes hypophosphorylated during splicing both in vivo and in vitro. TAP preferentially binds spliced mRNA-protein complexes compared with pre-mRNA-protein complexes. Thus, the phosphorylation state of the SR protein adapters may underlie the selectivity of TAP-mediated export of spliced mRNA.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
ARN Mensajero
/
Proteínas Nucleares
/
Empalme del ARN
/
Proteínas de Unión al ARN
/
Proteínas de Transporte Nucleocitoplasmático
/
Transporte de ARN
Límite:
Humans
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
2004
Tipo del documento:
Article
País de afiliación:
Estados Unidos