Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Hek-293t Cell
SUBMITTER: Federico Uliana
LAB HEAD: Matthias Gstaiger
PROVIDER: PXD012378 | Pride | 2019-04-02
REPOSITORIES: Pride
Items per page: 1 - 5 of 37 |
Nature communications 20190215 1
Serine/threonine phosphatases such as PP1 lack substrate specificity and associate with a large array of targeting subunits to achieve the requisite selectivity. The tumour suppressor ASPP (apoptosis-stimulating protein of p53) proteins associate with PP1 catalytic subunits and are implicated in multiple functions from transcriptional regulation to cell junction remodelling. Here we show that Drosophila ASPP is part of a multiprotein PP1 complex and that PP1 association is necessary for several ...[more]