ArticleThe FEBS journal2026
Synthetic trap-peptides identify a TOM complex phosphatase - PP2A dephosphorylates Tom6.
Article in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Endogenous RALF peptide function is required for powdery mildew host colonization.The New phytologist · 2026Article
- Protocol to study direct (de)phosphorylation events on a proteome-wide scale using on-bead in vitro enzyme assays.STAR protocols · 2026Article
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Authors and funding
8 authors.
Funding
Abstract
The identification of phosphatases that dephosphorylate specific sites in proteins remains a major challenge, particularly for the major class of serine/threonine-specific phosphatases, which function as holoenzymes. Here, we report the development of synthetic trap-peptides to identify phosphatases that bind to Tom6, a subunit of the mitochondrial translocase of the outer membrane (TOM) complex. The TOM complex is regulated by reversible phosphorylation, and although responsible kinases have been identified, the corresponding phosphatases so far remain unknown. Here, the trap-peptides enriched phosphoserine/threonine-specific protein phosphatases 2A (PP2A) and 4 (PP4) as full holoenzymes from yeast cytosolic fractions. We observed that their interaction with Tom6 was mediated through their regulatory subunits Cdc55
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