Journal of Cancer Prevention

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Fig. 2.

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Fig. 2. ERK2 binds to F and linker domains of βTrCP1. (A) Amino acid alignment of putative ERKs docking sites in βTrCP1. MAPK docking sequence was noted in footnote. (B) Construction strategies for βTrCP1 truncated mutants. The mutants were recombined into pcDNA3-HA. (C) The constructs of (B) were co-transfected as indicated. (D) Construction strategies for βTrCP1 intradomain deletion mutants. The mutants were recombined into pcDNA3-HA. (E) Interaction domain deciphering of βTrCP1 to ERK2. The constructs in (D) were co-transfected as indicated. (C, E) The interaction of ERK2 and each of βTrCP1 mutants were visualized by IP/Western blotting as indicated. MKP3, mitogen-activated protein kinase phosphatase 3; ERK, extracellular signal-regulated kinase; PTPN5, protein-tyrosine phosphatase nonreceptor type 5; DUSP8, dual-specificity phosphatase 8; MEK1, MAP kinase kinase 1; RSK1, ribosomal S6 kinase 1; N. D., not determined; MAPK, mitogen-activated protein kinases; D, D domain; F, F-box domian; FL, full length; IP, immunoprecipitation; HA, Hemagglutinin; WCL, whole cell lysates, Xp, Xpress.
J Cancer Prev 2021;26:174~182
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