IndraLab

Statements

P14_3_3 binds KCNF1. 4 / 4
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sparser
"We also show that phospho-KH1 interacts directly and specifically with 14-3-3 in vitro and phosphorylation of Ser193 causes a 14-3-3-dependent alteration of the nuclear/cytoplasmic distribution of the protein."
19198587
sparser
"To confirm that this model is applicable to our data and to show that the 14-3-3-KH1 interaction is indeed mediated by a short unfolded and phosphorylated amino acid stretch we have used a 10-fold excess of a phospho-peptide that spans the KH1 14-3-3 target sequence (GLPERSVS p LTGAPES) to compete out 14-3-3 protein."
19198587
sparser
"The experiments described above show that KH1 interacts with 14-3-3 only when the domain is phosphorylated and unfolded and that, as we previously proposed xref , this interaction is mediated by a short target sequence within the domain."
19198587
sparser
"14-3-3–KH1 interaction regulates the mRNA decay activity of KSRP by sequestering the protein in a separate functional pool."
19198587