PMID- 10049757
OWN - NLM
STAT- MEDLINE
DCOM- 19990401
LR  - 20071115
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 255
IP  - 3
DP  - 1999 Feb 24
TI  - SRPK1 and LBR protein kinases show identical substrate specificities.
PG  - 602-7
AB  - Arginine/serine protein kinases constitute a novel class of enzymes that can
      modify arginine/serine (RS) dipeptide motifs. SR splicing factors that are
      essential for pre-mRNA splicing and the lamin B receptor (LBR), an integral
      protein of the inner nuclear membrane, are among the best characterized proteins 
      that contain RS domains. Two SR Protein-specific Kinases, SRPK1 and SRPK2, have
      been shown to phosphorylate specifically the RS motifs of the SR family of
      splicing factors and play an important role in regulating both the spliceosome
      assembly and their intranuclear distribution, whereas an LBR-associated kinase,
      that specifically phosphorylates a stretch of RS repeats located at the
      NH2-terminal region of LBR, has been recently purified and characterized from
      turkey erythrocyte nuclear envelopes. Using synthetic peptides representing
      different regions of LBR and recombinant proteins produced in bacteria we now
      demonstrate that SRPK1 modifies LBR with similar kinetics and on the same sites
      as the LBR kinase, that are also phosphorylated in vivo. These data provide
      significant evidence for a new role of SRPK1 in addition to that of pre-mRNA
      splicing.
CI  - Copyright 1999 Academic Press.
FAU - Papoutsopoulou, S
AU  - Papoutsopoulou S
AD  - Laboratory of Biochemistry, School of Chemistry, Aristotelian University of
      Thessaloniki, Thessaloniki, 54 006, Greece.
FAU - Nikolakaki, E
AU  - Nikolakaki E
FAU - Giannakouros, T
AU  - Giannakouros T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphopeptides)
RN  - 0 (RNA Precursors)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Recombinant Proteins)
RN  - 0 (lamin B receptor)
RN  - EC 2.7.1.- (SRPK1 protein, human)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Humans
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Nuclear Envelope/enzymology
MH  - Nuclear Proteins/metabolism
MH  - Phosphopeptides/analysis
MH  - Phosphorylation
MH  - Protein-Serine-Threonine Kinases/*metabolism
MH  - RNA Precursors/metabolism
MH  - RNA Splicing/genetics
MH  - Receptors, Cytoplasmic and Nuclear/*metabolism
MH  - Recombinant Proteins/metabolism
MH  - Substrate Specificity
MH  - Trypsin/metabolism
EDAT- 1999/03/02 00:00
MHDA- 1999/03/02 00:01
CRDT- 1999/03/02 00:00
PHST- 1999/03/02 00:00 [pubmed]
PHST- 1999/03/02 00:01 [medline]
PHST- 1999/03/02 00:00 [entrez]
AID - S0006-291X(99)90249-8 [pii]
AID - 10.1006/bbrc.1999.0249 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Feb 24;255(3):602-7. doi:
      10.1006/bbrc.1999.0249.