p(HGNC:PIN1, frag("5_39"))

Entity

Name

PIN1

Namespace

hgnc

Namespace Version

20180906

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/hgnc-names.belns

TAU Interactions Section of NESTOR

In contrast, no binding was observed between Pin1 and the nonphosphorylated tau (Fig. 4a), demonstrating that T231 phosphorylation is required for Pin1 binding of tau. To determine whether the WW domain of Pin1 is responsible for binding, the mutant Pin1Y23A was used, which contains a single alanine substitution at the critical Tyr 23 in theWWdomain, resulting in a loss of the phosphoserine-binding activity13. Pin1Y23A showed much less binding to pT231 peptide (Table 1). The residual binding might be due to binding of the pT231 peptide to the much lower affinity isomerase domain of Pin113. These results indicate that the WW domain mediates Pin1 binding to the pT231 sequence of tau. PubMed:10391244

In contrast, no binding was observed between Pin1 and the nonphosphorylated tau (Fig. 4a), demonstrating that T231 phosphorylation is required for Pin1 binding of tau. To determine whether the WW domain of Pin1 is responsible for binding, the mutant Pin1Y23A was used, which contains a single alanine substitution at the critical Tyr 23 in theWWdomain, resulting in a loss of the phosphoserine-binding activity13. Pin1Y23A showed much less binding to pT231 peptide (Table 1). The residual binding might be due to binding of the pT231 peptide to the much lower affinity isomerase domain of Pin113. These results indicate that the WW domain mediates Pin1 binding to the pT231 sequence of tau. PubMed:10391244

In contrast, no binding was observed between Pin1 and the nonphosphorylated tau (Fig. 4a), demonstrating that T231 phosphorylation is required for Pin1 binding of tau. To determine whether the WW domain of Pin1 is responsible for binding, the mutant Pin1Y23A was used, which contains a single alanine substitution at the critical Tyr 23 in theWWdomain, resulting in a loss of the phosphoserine-binding activity13. Pin1Y23A showed much less binding to pT231 peptide (Table 1). The residual binding might be due to binding of the pT231 peptide to the much lower affinity isomerase domain of Pin113. These results indicate that the WW domain mediates Pin1 binding to the pT231 sequence of tau. PubMed:10391244

In contrast, no binding was observed between Pin1 and the nonphosphorylated tau (Fig. 4a), demonstrating that T231 phosphorylation is required for Pin1 binding of tau. To determine whether the WW domain of Pin1 is responsible for binding, the mutant Pin1Y23A was used, which contains a single alanine substitution at the critical Tyr 23 in theWWdomain, resulting in a loss of the phosphoserine-binding activity13. Pin1Y23A showed much less binding to pT231 peptide (Table 1). The residual binding might be due to binding of the pT231 peptide to the much lower affinity isomerase domain of Pin113. These results indicate that the WW domain mediates Pin1 binding to the pT231 sequence of tau. PubMed:10391244

In contrast, no binding was observed between Pin1 and the nonphosphorylated tau (Fig. 4a), demonstrating that T231 phosphorylation is required for Pin1 binding of tau. To determine whether the WW domain of Pin1 is responsible for binding, the mutant Pin1Y23A was used, which contains a single alanine substitution at the critical Tyr 23 in theWWdomain, resulting in a loss of the phosphoserine-binding activity13. Pin1Y23A showed much less binding to pT231 peptide (Table 1). The residual binding might be due to binding of the pT231 peptide to the much lower affinity isomerase domain of Pin113. These results indicate that the WW domain mediates Pin1 binding to the pT231 sequence of tau. PubMed:10391244