The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Regulated protein–protein interaction between aPKC and PAR‐3 plays an essential role in the polarization of epithelial cells
Open accessAbstract
Background: Recent studies have revealed that aPKC (atypical protein kinase C), PAR‐3 and PAR‐6 play indispensable roles in the regulation of various cell polarization events, from worms to mammals, suggesting that they comprise an evolutionarily conserved protein machinery which is essential for cell polarization. The three proteins interact with each other to form a ternary complex and thus mutually regulate their functionality and localization. Here, we investigated the biochemical nature of the aPKC–PAR‐3 interaction in detail to clarify its functional importance in cell polarity. Results: The highly conserved 26 amino acid sequence 816–841, in PAR‐3 was found to be necessary and sufficient for the tight association with aPKC. Among several conserved serine/threonine residues within the region, aPKC preferentially phosphorylates serine‐827 in vitro, and this phosphorylation reduces the stability of the PAR‐3–aPKC interaction. Several analyses using a phospho‐serine 827 specific antibody have established that this phosphorylation by aPKC occurs in vivo. Over‐expression of a point mutant of PAR‐3 (S827A), which is predicted to form a stable complex with aPKC, causes defects in the cell‐cell contact‐induced cell polarization of epithelial MDCK cells, similarly to a dominant negative mutant of aPKC. Conclusions: These results imply that serine 827 in the aPKC binding site of PAR‐3 is a target of aPKC and that the regulated interaction between a protein kinase, aPKC, and its substrate, PAR‐3, plays an essential role in the establishment of cell polarity.
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Cites
The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
Joberty, G., Petersen, C., Gao, L., & Macara, I. G. (2000) · Nature Cell Biology · doi:10.1038/35019573 · Cited by 928 · cited 3×
“However, some laboratories have reported a direct interaction between the isolated PDZ domain of PAR-6 and the PDZ domains of PAR-3 in its deletion mutants or an isoform lacking the C-terminal region ( Joberty et al. 2000; Lin et al. 2000).”
A mammalian PAR-3–PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
Lin, D., Edwards, A. S., Fawcett, J. P., Mbamalu, G., Scott, J. D., & Pawson, T. (2000) · Nature Cell Biology · doi:10.1038/35019582 · Cited by 743
Yamanaka, T., Horikoshi, Y., Suzuki, A., Sugiyama, Y., Kitamura, K., Maniwa, R., Nagai, Y., Yamashita, A., Hirose, T., Ishikawa, H., et al. (2001) · Genes to Cells · doi:10.1046/j.1365-2443.2001.00453.x · Cited by 306
Self-citationSuzuki, A., Ishiyama, C., Hashiba, K., Shimizu, M., Ebnet, K., & Ohno, S. (2002) · Journal of Cell Science · doi:10.1242/jcs.00032 · Cited by 251
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Cited by
Coordinated protein sorting, targeting and distribution in polarized cells
Mellman, I., & Nelson, W. J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2525 · Cited by 521
Assémat, E., Bazellières, E., Pallesi-Pocachard, E., Le Bivic, A., & Massey-Harroche, D. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.08.029 · Cited by 470
Benton, R., & Johnston, D. S. (2003) · Cell · doi:10.1016/s0092-8674(03)00938-3 · Cited by 410
Wirtz-Peitz, F., Nishimura, T., & Knoblich, J. A. (2008) · Cell · doi:10.1016/j.cell.2008.07.049 · Cited by 369
Macara, I. G. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1332 · Cited by 341
Metadata
- Authors
- Nagai‐Tamai, Y., Mizuno, K., Hirose, T., Suzuki, A., & Ohno, S.
- Venue
- Genes to Cells
- Publisher
- Wiley
- Published
- 2002-10-17
- Volume
- 7
- Issue
- 11
- Pages
- 1161-1171
- ISSN
- 1356-9597 (ISSN-L)
- 1365-2443
- OpenAlex
- W2160863855
- Cited by
- 192
- References
- 4
- FWCI
- 1.84
- Type
- journal article
- Language
- en
- Open access
- bronze
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