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MAPK1 phosphorylates EIF4EBP1. 13 / 13
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"In order to assure maximal phosphorylation of 4E-BP1 by ERK2, 1.6 mug of 4E-BP1 was phosphorylated using 375 U of ERK2."
11404183
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"However, unlike earlier studies, which relied on various methods to separate free eIF4E from 4E-BP1-bound eIF4E or required isolation of the 4E, BP1, and eIF4E complex, FRET allows for a direct determ[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
11404183
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"Since ERK2 only phosphorylates free 4E-BP1, this finding suggests that phosphorylation by CK-II does not cause dissociation of the 4E-BP1–eIF4E complex."
11404183
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"This point is illustrated in the present study by the observation that addition of GFP variants to eIF4E and 4E-BP1 does not prevent their interaction or interfere with phosphorylation of EYFP–4E-BP1 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
11404183
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"In order to assure maximal phosphorylation of 4E-BP1 by ERK2, 1.6 μg of 4E-BP1 was phosphorylated using 375 U of ERK2."
11404183
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"The phosphorylated ERK2 then can further phosphorylate PHAS-I efficiently (lane 7), whereas non-phosphorylated ERK2 cannot phosphorylate PHAS-I (lane 8)."
9373147
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"Thus, when 4E-BP1-eIF4E is used as substrate, ERK2 is unable to phosphorylate 4E-BP1 regardless of whether or not it has been earlier phosphorylated by CK-II."
11404183
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"In contrast, activated recombinant ERK2 phosphorylated both wild-type 4E-BP1 [17] and the TOS motif mutant F114A to a similar extent, indicating that the proline directed sites in both recombinant pro[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12747827
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"Phosphorylation of EYFP--4E-BP1 by the mitogen-activated protein kinase ERK2, but not by casein kinase CK-II, also attenuated the interaction."
11404183
reach
"Since ERK2 only phosphorylates free 4E-BP1, this finding suggests that phosphorylation by CK-II does not cause dissociation of the 4E, BP1, and eIF4E complex."
11404183
sparser
"In contrast, activated recombinant ERK2 phosphorylated both wild-type 4E-BP1 and the TOS motif mutant F114A to a similar extent , indicating that the proline-directed sites in both recombinant protei[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12747827
sparser
"Thus, when 4E-BP1–eIF4E is used as substrate, ERK2 is unable to phosphorylate 4E-BP1 regardless of whether or not it has been earlier phosphorylated by CK-II."
11404183
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"First, in contrast to MAPK1, which has been shown to phosphorylate 4EBP1 in vitro XREF_BIBR, we are not aware of any evidence that MAPK3 can directly phosphorylate 4E-BP1."
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