| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-73 |
Sentence |
denotes |
Cloning and characterization of RLPK, a novel RSK-related protein kinase. |
| T2 |
74-178 |
Sentence |
denotes |
A novel protein kinase whose activity can be stimulated by mitogen in vivo was cloned and characterized. |
| T3 |
179-348 |
Sentence |
denotes |
The cDNA of this gene encodes an 802-amino acid protein (termed RLPK) with the highest homology (37% identity) to the two protein kinase families, p90(RSK) and p70(RSK). |
| T4 |
349-450 |
Sentence |
denotes |
Like p90(RSR), but not p70(RSK), RLPK also contains two complete nonidentical protein kinase domains. |
| T5 |
451-561 |
Sentence |
denotes |
RLPK mRNA is widely expressed in all human tissues examined and is enriched in the brain, heart, and placenta. |
| T6 |
562-812 |
Sentence |
denotes |
In HeLa cells, transiently expressed epitope-tagged RLPK can be strongly induced by epidermal growth factor, serum, and phorbol 12-myristate 13-acetate, but only moderately up-regulated by tumor necrosis factor-alpha and other stress-related stimuli. |
| T7 |
813-1172 |
Sentence |
denotes |
The activity of RLPK stimulated by epidermal growth factor was not inhibited by several known protein kinase C inhibitors nor by rapamycin, a known specific inhibitor for p70(RSK), but could be inhibited by herbimycin A, a tyrosine kinase inhibitor, and partially inhibited by PD98059 or SB203580, inhibitors for the mitogen-activated protein kinase pathways. |
| T8 |
1173-1278 |
Sentence |
denotes |
Recombinant RLPK possesses high phosphorylation activity toward histone 2B and the S6 peptide, RRRLSSLRA. |
| T9 |
1279-1420 |
Sentence |
denotes |
Although purified recombinant RLPK can be phosphorylated by ERK2 and p38alpha in vitro, its activity is not affected by this phosphorylation. |
| T10 |
1421-1519 |
Sentence |
denotes |
Moreover, the treatment of RLPK with acid phosphatase did not reduce its in vitro kinase activity. |
| T11 |
1520-1681 |
Sentence |
denotes |
These data suggest that RLPK is structurally similar to previously isolated RSKs, but its regulatory mechanism may be distinct from either p70(RSK) or p90(RSK)s. |