An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

Publication

The PHLPP1 N-Terminal Extension is a Mitotic Cdk1 Substrate and Controls an Interactome Switch.

Kawashima AT, Wong C, Lorden G, King CC, Lara-Gonzalez P, Desai A, Gingras AC, Newton AC

PH domain Leucine-Rich Repeat Protein Phosphatase 1 (PHLPP1) is a tumor suppressor that directly dephosphorylates a wide array of substrates, most notably the pro-survival kinase Akt. However, little is known about the molecular mechanisms governing PHLPP1 itself. Here we report that PHLPP1 is dynamically regulated in a cell cycle-dependent manner, and deletion of PHLPP1 results in mitotic delays and increased ... [more]

Mol Cell Biol Jan. 04, 2021; (); [Pubmed: 33397691]

Throughput

High Throughput

Additional Notes

BioID
No nocodazole treatment
Nocodazole treated cells
PHLPP1 wildtype
Saint express was used to identify proximity interactions and those with a BFRD of <= 1% were considered high confidence
deltaNTE (N terminal extension of PHLPP1 deleted)

Curated By

BioGRID

Interaction Summary

PHLPP1

Gene Ontology Biological Process

Gene Ontology Molecular Function

protein binding [IPI]

Gene Ontology Cellular Component

EEF1D