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PubMed:21098038 JSONTXT 21 Projects

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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.