Fyn Phosphorylates Human MAP-2c on Tyrosine 67
Copyright policy )Fyn Phosphorylates Human MAP-2c on Tyrosine 67
The Src homology 3 (SH3) domain of Fyn binds to a conserved PXXP motif on microtubule-associated protein-2. Co-transfections into COS7 cells and in vitro kinase assays performed with Fyn and wild-type, or mutant MAP-2c, determined that Fyn phosphorylated MAP-2c on tyrosine 67. The phosphorylation generated a consensus sequence for the binding of the SH2 domain of Grb2 (pYSN). Pull-down assays with SH2-Grb2 from human fetal brain homogenates, and co-immunoprecipitation of Grb2 and MAP-2 confirmed the interaction in vivo, and demonstrated that MAP-2c is tyrosine-phosphorylated in human fetal brain. Filter overlay assays confirmed that the SH2 domain of Grb2 binds to human MAP-2c following incubation with active Fyn. Enzyme-linked immunosorbent assays confirmed the interaction between the SH2 domain of Grb2 and a tyrosine-phosphorylated MAP-2 peptide spanning the pY(67)SN motif. Thus, MAP-2c can directly recruit multiple signaling proteins important for central nervous system development.
- Albert Einstein College of Medicine United States
Binding Sites, Base Sequence, Amino Acid Motifs, Proto-Oncogene Proteins c-fyn, src Homology Domains, src-Family Kinases, Proto-Oncogene Proteins, Humans, Tyrosine, Phosphorylation, Microtubule-Associated Proteins, Adaptor Proteins, Signal Transducing, DNA Primers, GRB2 Adaptor Protein
Binding Sites, Base Sequence, Amino Acid Motifs, Proto-Oncogene Proteins c-fyn, src Homology Domains, src-Family Kinases, Proto-Oncogene Proteins, Humans, Tyrosine, Phosphorylation, Microtubule-Associated Proteins, Adaptor Proteins, Signal Transducing, DNA Primers, GRB2 Adaptor Protein
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