ArticleNature communications2017
The Par3 polarity protein is an exocyst receptor essential for mammary cell survival.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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Who cites it
40 citing papers in PubMed, 77 citations in OpenAlex.
- Centrosome migration and apical membrane formation during epithelial polarization in MDCK cysts.eLife · 2026Article
- Semaphorin 3A-mediated perineuronal nets formation incubates depressive-like behaviors in male mice via activating parvalbumin-expressing interneurons.Molecular psychiatry · 2026Article
- Non-canonical EGFR signaling promotes MAPK-dependent extrusion of epithelial cells.Journal of cell science · 2025Article
- Confinement promotes nematic alignment of spindle-shaped cells during Drosophila embryogenesis.Development (Cambridge, England) · 2024Article
- DCAF1 interacts with PARD3 to promote hepatocellular carcinoma progression and metastasis by activating the Akt signaling pathway.Journal of experimental & clinical cancer research : CR · 2024Article
- Polarity protein AF6 functions as a modulator of necroptosis by regulating ubiquitination of RIPK1 in liver diseases.Cell death & disease · 2023Article
- A junction-dependent mechanism drives murine mammary cell intercalation for ductal elongation.Developmental cell · 2023Article
- Multicellular rosettes link mesenchymal-epithelial transition to radial intercalation in the mouse axial mesoderm.Developmental cell · 2023Article
- The exocyst complex is required for the trafficking and delivery of KCa3.1 to the basolateral membrane of polarized epithelia.American journal of physiology. Cell physiology · 2023Article
- A comprehensive review of the ten main platelet receptors involved in platelet activity and cardiovascular disease.American journal of blood research · 2023Review
- Listeria monocytogenes Co-Opts the Host Exocyst Complex To Promote Internalin A-Mediated Entry.Infection and immunity · 2022Article
- Regulation of EGF-stimulated activation of the PI-3K/AKT pathway by exocyst-mediated exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Apical-basal polarity and the control of epithelial form and function.Nature reviews. Molecular cell biology · 2022Review
- A mechanism for exocyst-mediated tethering via Arf6 and PIP5K1C-driven phosphoinositide conversion.Current biology : CB · 2022Article
- Plasma membrane phosphatidylinositol (4,5)-bisphosphate is critical for determination of epithelial characteristics.Nature communications · 2022Article
- Kinesin-directed secretion of basement membrane proteins to a subdomain of the basolateral surface in Drosophila epithelial cells.Current biology : CB · 2022Article
- Par-3 family proteins in cell polarity & adhesion.The FEBS journal · 2022Review
- Rho and Rab Family Small GTPases in the Regulation of Membrane Polarity in Epithelial Cells.Frontiers in cell and developmental biology · 2022Review
- RASSF8-mediated transport of Echinoid via the exocyst promotes Drosophila wing elongation and epithelial ordering.Development (Cambridge, England) · 2021Article
- Par3 cooperates with Sanpodo for the assembly of Notch clusters following asymmetric division ofeLife · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The exocyst is an essential component of the secretory pathway required for delivery of basolateral proteins to the plasma membranes of epithelial cells. Delivery occurs adjacent to tight junctions (TJ), suggesting that it recognizes a receptor at this location. However, no such receptor has been identified. The Par3 polarity protein associates with TJs but has no known function in membrane traffic. We now show that, unexpectedly, Par3 is essential for mammary cell survival. Par3 silencing causes apoptosis, triggered by phosphoinositide trisphosphate depletion and decreased Akt phosphorylation, resulting from failure of the exocyst to deliver basolateral proteins to the cortex. A small region of PAR3 binds directly to Exo70 and is sufficient for exocyst docking, membrane-protein delivery and cell survival. PAR3 lacking this domain can associate with the cortex but cannot support exocyst function. We conclude that Par3 is the long-sought exocyst receptor required for targeted membrane-protein delivery.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.