Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Interactor-mediated nuclear translocation and retention of protein phosphatase-1.

The Journal of biological chemistry - 31 Dec 2004

Lesage Bart, Beullens Monique, Nuytten Mieke, Van Eynde Aleyde, Keppens Stefaan, Himpens Bernard, Bollen Mathieu

Abstract excerpt

Protein Ser/Thr phosphatase-1 (PP1) is a ubiquitous eukaryotic enzyme that controls numerous cellular processes by the dephosphorylation of key regulatory proteins. PP1 is expressed in various cellular compartments but is most abundant in the nucleus. We have examined the determinants for the nuclear localization of enhanced green fluorescent protein-tagged PP1 in COS1 cells. Our studies show that PP1gamma(1)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Histidine
Share to Active Transport, Cell Nucleus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endoribonucleases

Share to Immunoprecipitation

Share to Nuclear Localization Signals

Share to Phosphoprotein Phosphatases

Share to Protein Phosphatase 1

Share to Threonine

Source

Identifiers

PMID: 15501817
DOI: 10.1074/jbc.M411911200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interactor-mediated nuclear translocation and retention of protein phosphatase-1.PMID 15501817Read ↗

NOM1 targets protein phosphatase I to the nucleolus.Semantic proximity Read ↗

The nuclear scaffold protein NIPP1 is essential for early embryonic development and cell proliferation.Semantic proximity Read ↗

Repo-Man recruits PP1 gamma to chromatin and is essential for cell viability.Semantic proximity Read ↗

Importance of a surface hydrophobic pocket on protein phosphatase-1 catalytic subunit in recognizing cellular regulators.Semantic proximity Read ↗

Protein phosphatase PP1-NIPP1 activates mesenchymal genes in HeLa cells.Semantic proximity Read ↗

Identification of a nuclear localization signal, RRMKWKK, in the homeodomain transcription factor PDX‐1Semantic proximity Read ↗

The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding.Semantic proximity Read ↗

Nuclear export and centrosome targeting of the protein phosphatase 2A subunit B56alpha: role of B56alpha in nuclear export of the catalytic subunit.Semantic proximity Read ↗

Cytoplasmic targeting of mutant poly(A)-binding protein nuclear 1 suppresses protein aggregation and toxicity in oculopharyngeal muscular dystrophy.Semantic proximity Read ↗

Phosphoregulation of Arp2/3-dependent actin assembly during receptor-mediated endocytosis.Semantic proximity Read ↗

Acetylation regulates subcellular localization of the Wnt signaling nuclear effector POP-1.Semantic proximity Read ↗

Phosphorylation of Varicella-Zoster Virus IE63 Protein by Casein Kinases Influences Its Cellular Localization and Gene Regulation ActivitySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.