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

Direct association of Bazooka/PAR-3 with the lipid phosphatase PTEN reveals a link between the PAR/aPKC complex and phosphoinositide signaling.

Development (Cambridge, England) - 1 Apr 2005

von Stein Walter, Ramrath Andreas, Grimm Alexandra, Müller-Borg Marion, Wodarz Andreas

Abstract excerpt

Cell polarity in Drosophila epithelia, oocytes and neuroblasts is controlled by the evolutionarily conserved PAR/aPKC complex, which consists of the serine-threonine protein kinase aPKC and the PDZ-domain proteins Bazooka (Baz) and PAR-6. The PAR/aPKC complex is required for the separation of apical and basolateral plasma membrane domains, for the asymmetric localization of cell fate determinants and for the...

Read the complete abstract on PubMed

Topics

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

Share to Cytoskeleton
Share to Epithelium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oocytes

Share to Phosphatidylinositols

Share to Phosphoric Monoester Hydrolases

Share to Protein Kinase C

Share to PTEN Phosphohydrolase

Share to Two-Hybrid System Techniques

Source

Identifiers

PMID: 15743877
DOI: 10.1242/dev.01720

Genes

PTEN

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Direct association of Bazooka/PAR-3 with the lipid phosphatase PTEN reveals a link between the PAR/aPKC complex and phosphoinositide signaling.PMID 15743877Read ↗

Membrane targeting of Bazooka/PAR-3 is mediated by direct binding to phosphoinositide lipids.Semantic proximity Read ↗

Bazooka and atypical protein kinase C are required to regulate oocyte differentiation in the <i>Drosophila</i> ovarySemantic proximity Read ↗

PP2A antagonizes phosphorylation of Bazooka by PAR-1 to control apical-basal polarity in dividing embryonic neuroblasts.Semantic proximity Read ↗

Bazooka is required for polarisation of the Drosophila anterior-posterior axis.Semantic proximity Read ↗

Interactions between the PDZ domains of Bazooka (Par-3) and phosphatidic acid: in vitro characterization and role in epithelial development.Semantic proximity Read ↗

Kinase-activity-independent functions of atypical protein kinase C in Drosophila.Semantic proximity Read ↗

Control of spindle orientation in Drosophila by the Par-3-related PDZ-domain protein Bazooka.Semantic proximity Read ↗

Drosophila aPKC regulates cell polarity and cell proliferation in neuroblasts and epithelia.Semantic proximity Read ↗

Par‐3 family proteins in cell polarity & adhesionSemantic proximity Read ↗

Redundant regulation of localization and protein stability of DmPar3.Semantic proximity Read ↗

Slmb antagonises the aPKC/Par-6 complex to control oocyte and epithelial polarity.Semantic proximity Read ↗

A Cdc42-regulated actin cytoskeleton mediates Drosophila oocyte polarization.Semantic proximity Read ↗

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