Peptide probes containing a non‐hydrolyzable phosphotyrosine‐mimetic residue for enrichment of protein tyrosine phosphatases

We developed peptide probes containing a non‐hydrolyzable phosphotyrosine mimetic, 4‐[difluoro(phosphono)methyl]‐L‐phenylalanine (F2Pmp) for the enrichment of protein tyrosine phosphatases (PTPs). We found that different F2Pmp probes can enrich different PTPs, depending on the probe sequence. Furthe...

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Bibliographic Details
Published in:Proteomics (Weinheim) 2022-02, Vol.22 (4), p.e2100144-n/a
Main Authors: Tsumagari, Kazuya, Niinae, Tomoya, Otaka, Akira, Ishihama, Yasushi
Format: Article
Language:English
Subjects:
Antibodies
Dephosphorylation
Enrichment
F2Pmp
Homology
peptide probe
Peptides
Phenylalanine
Phosphatase
Phosphotyrosine
Probes
Proteins
PTP
pulldown
Tyrosine
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Summary:We developed peptide probes containing a non‐hydrolyzable phosphotyrosine mimetic, 4‐[difluoro(phosphono)methyl]‐L‐phenylalanine (F2Pmp) for the enrichment of protein tyrosine phosphatases (PTPs). We found that different F2Pmp probes can enrich different PTPs, depending on the probe sequence. Furthermore, proteins containing a Src homology 2 (SH2) domain were enriched together. Importantly, probes containing phosphotyrosine instead of F2Pmp failed to enrich PTPs due to dephosphorylation during the pulldown step. This enrichment approach using peptides containing F2Pmp could be a generic tool for tyrosine phosphatome analysis without the use of antibodies.
ISSN:1615-9853
1615-9861
DOI:10.1002/pmic.202100144