| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-146 |
Sentence |
denotes |
Quantitative analysis of ERK2 interactions with substrate proteins: roles for kinase docking domains and activity in determining binding affinity. |
| T2 |
147-363 |
Sentence |
denotes |
Extracellular signal-regulated kinase-1 and -2 (ERK1/2) proteins regulate a variety of cellular functions, including cell proliferation and differentiation, by interacting with and phosphorylating substrate proteins. |
| T3 |
364-485 |
Sentence |
denotes |
Two docking sites, common docking (CD/ED) domain and F-site recruitment site (FRS), on ERK proteins have been identified. |
| T4 |
486-702 |
Sentence |
denotes |
Specific interactions with the CD/ED domain and the FRS occur with substrates containing a docking site for ERK and JNK, LXL (DEJL) motif (D-domain) and a docking site for ERK, FXF (DEF) motif (F-site), respectively. |
| T5 |
703-860 |
Sentence |
denotes |
However, the relative contributions of the ERK docking sites in mediating substrate interactions that allow efficient phosphate transfer are largely unknown. |
| T6 |
861-1033 |
Sentence |
denotes |
In these studies, we provide a quantitative analysis of ERK2 interactions with substrates using surface plasmon resonance to measure real time protein-protein interactions. |
| T7 |
1034-1184 |
Sentence |
denotes |
ERK2 interacted with ELK-1 (DEF and DEJL motifs), RSK-1 (DEJL motif), and c-Fos (DEF motif) with K(D) values of 0.25, 0.15, and 0.97 μM, respectively. |
| T8 |
1185-1307 |
Sentence |
denotes |
CD/ED domain mutations inhibited interactions with ELK-1 and RSK-1 by 6-fold but had no effect on interactions with c-Fos. |
| T9 |
1308-1448 |
Sentence |
denotes |
Select mutations in FRS residues differentially inhibited ELK-1 or c-Fos interactions with ERK2 but had little effect on RSK-1 interactions. |
| T10 |
1449-1632 |
Sentence |
denotes |
Mutations in both the ED and FRS docking sites completely inhibited ELK-1 interactions but had no effect on interactions with stathmin, an ERK substrate whose docking site is unknown. |
| T11 |
1633-1769 |
Sentence |
denotes |
The phosphorylation status of ERK2 did not affect interactions with RSK-1 or c-Fos but did inhibit interactions with ELK-1 and stathmin. |
| T12 |
1770-1990 |
Sentence |
denotes |
These studies provide a quantitative evaluation of specific docking domains involved in mediating interactions between ERK2 and protein substrates and define the contributions of these interactions to phosphate transfer. |
