期刊
JOURNAL OF CELL BIOLOGY
卷 200, 期 5, 页码 635-650出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201208150
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资金
- MEXT (the Ministry of Education, Culture, Sports, Science and Technology) KAKENHI [20117002]
- Targeted Proteins Research Program (TPRP) from MEXT
- JSPS (Japan Society for the Promotion of Science) KAKENHI [24590385]
- Grants-in-Aid for Scientific Research [24590385, 20117002] Funding Source: KAKEN
Formation of apico-basal polarity in epithelial cells is crucial for both morphogenesis (e.g., cyst formation) and function (e.g., tight junction development). Atypical protein kinase C (aPKC), complexed with Par6, is considered to translocate to the apical membrane and function in epithelial cell polarization. However, the mechanism for translocation of the Par6-aPKC complex has remained largely unknown. Here, we show that the WD40 protein Morg1 (mitogen-activated protein kinase organizer 1) directly binds to Par6 and thus facilitates apical targeting of Par6-aPKC in Madin-Darby canine kidney epithelial cells. Morg1 also interacts with the apical transmembrane protein Crumbs3 to promote Par6-aPKC binding to Crumbs3, which is reinforced with the apically localized small GTPase Cdc42. Depletion of Morg1 disrupted both tight junction development in monolayer culture and cyst formation in three-dimensional culture; apico-basal polarity was notably restored by forced targeting of aPKC to the apical surface. Thus, Par6-aPKC recruitment to the premature apical membrane appears to be required for definition of apical identity of epithelial cells.
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