Distinct mechanisms govern the phosphorylation of different SR protein splicing factors.
RNA splicing
SR protein
SRPK
SRSF
kinase-substrate interaction
localization
nuclear speckle
phosphoryl transfer
post-translational mechanism
post-translational modification (PTM)
processive phosphorylation
protein kinase
protein phosphorylation
regulatory mechanism
serine/threonine protein kinase
speckles
subcellular localization
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
25 01 2019
25 01 2019
Historique:
received:
10
04
2018
revised:
17
11
2018
pubmed:
28
11
2018
medline:
9
5
2019
entrez:
28
11
2018
Statut:
ppublish
Résumé
Serine-arginine (SR) proteins are essential splicing factors containing a canonical RNA recognition motif (RRM), sometimes followed by a pseudo-RRM, and a C-terminal arginine/serine-rich (RS) domain that undergoes multisite phosphorylation. Phosphorylation regulates the localization and activity of SR proteins, and thus may provide insight into their differential biological roles. The phosphorylation mechanism of the prototypic SRSF1 by serine-arginine protein kinase 1 (SRPK1) has been well-studied, but little is known about the phosphorylation of other SR protein members. In the present study, interaction and kinetic assays unveiled how SRSF1 and the single RRM-containing SRSF3 are phosphorylated by SRPK2, another member of the SRPK family. We showed that a conserved SRPK-specific substrate-docking groove in SRPK2 impacts the binding and phosphorylation of both SR proteins, and the localization of SRSF3. We identified a nonconserved residue within the groove that affects the kinase processivity. We demonstrated that, in contrast to SRSF1, for which SRPK-mediated phosphorylation is confined to the N-terminal region of the RS domain, SRSF3 phosphorylation sites are spread throughout its entire RS domain
Identifiants
pubmed: 30478176
pii: S0021-9258(20)38868-2
doi: 10.1074/jbc.RA118.003392
pmc: PMC6349114
pii:
doi:
Substances chimiques
SRSF1 protein, human
0
SRSF3 protein, human
0
Serine-Arginine Splicing Factors
170974-22-8
Protein Serine-Threonine Kinases
EC 2.7.11.1
SRPK2 protein, human
EC 2.7.11.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1312-1327Informations de copyright
© 2019 Long et al.
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