DataSets / Project home (Phosphatases in mitosis)
Phenotypic and Interaction Profiling of the Human Phosphatases Identifies Diverse Mitotic Regulators
First Author: Nicole St-Denis (see complete author list under
Abstract:
  Reversible phosphorylation is a fundamental regulatory mechanism, intricately coordinated by kinases and phosphatases, two classes of enzymes widely disrupted in human disease. To better understand the functions of the relatively understudied phosphatases, we have used complementary affinity purification and proximity-based interaction proteomics approaches to generate a physical interactome for 140 human proteins harboring phosphatase catalytic domains. We identified 1,335 high-confidence interactions (1,104 previously unreported), implicating these phosphatases in the regulation of a variety of cellular processes. Systematic phenotypic profiling of phosphatase catalytic and regulatory subunits revealed that phosphatases from every evolutionary family impinge on mitosis. Using clues from the interactome, we have uncovered unsuspected roles for DUSP19 in mitotic exit, CDC14A in regulating microtubule integrity, PTPRF in mitotic retraction fiber integrity, and DUSP23 in centriole duplication. The functional phosphatase interactome further provides a rich resource for ascribing functions for this important class of enzymes.

Navigating this website

• See the manuscript in Cell Reports

• The data included here is by default filtered at 1% FDR as calculated by SAINTexpress; unselect the "high confidence" buttons to view all data. To see those BioID proximity interactions that additionally scored high on the specificity filter, please refer instead to the Supplementary data (left).

• Select "Explore baits" (left) to view all baits profiled, organized alphabetically (view as a list), on sequence homology trees (view as a picture) or in historical phosphatase families as per DEPOD (view by category). Clicking on a bait will retrieve all its interactors (high confidence by default) and indicates which interactions are already deposited in the BioGRID and IntAct databases. Also see the many links to excellent external resources for the baits and/or preys, including ProteinAtlas, ProteomicsDB, NCBI Gene, GeneCards and UniProt.

• Search for a bait or prey by Official Gene Symbol through the "Search" tab on left (or at the top). You will be able to search across all projects you have access to.

• This manuscript is associated with a lot of Supplementary data, including figures, tables (notably the BioID data reanalyzed with the "Specificity" filter) and inputs for Cytoscape or prohits-viz.

• The phosphatase interactome project is a work in progress and the Gingras laboratory continues to clone, express, and map interactions for phosphatase clone variants. See our current list in "Supplementary Data".

• Note that the mass spectrometry data has been deposited at MassIVE (identifiers MSV000079889, MSV000079891, and MSV000079890); login with username "Mitosis", password "Phosphatases".

Please contact Anne-Claude (gingras@lunenfeld.ca) for questions.


Copyright © 2012 Gingras labs, Lunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital.