期刊
MOLECULAR BIOLOGY OF THE CELL
卷 25, 期 23, 页码 3749-3764出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E14-05-0968
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资金
- National Institutes of Health [R37 AR43380]
- J.L. Mayberry Endowment [AR041836, CA122151]
- Dermatology Foundation Career Development Grant
- Skin Cancer Foundation Paul Silberberg
- Cancer Center [P30 CA060553]
- National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases [5P30AR057216-02]
The pathways driving desmosome and adherens junction assembly are temporally and spatially coordinated, but how they are functionally coupled is poorly understood. Here we show that the Armadillo protein plakophilin 3 (Pkp3) mediates both desmosome assembly and E-cadherin maturation through Rap1 GTPase, thus functioning in a manner distinct from the closely related plakophilin 2 (Pkp2). Whereas Pkp2 and Pkp3 share the ability to mediate the initial phase of desmoplakin (DP) accumulation at sites of cell-cell contact, they play distinct roles in later steps: Pkp3 is required for assembly of a cytoplasmic population of DP-enriched junction precursors, whereas Pkp2 is required for transfer of the precursors to the membrane. Moreover, Pkp3 forms a complex with Rap1 GTPase, promoting its activation and facilitating desmosome assembly. We show further that Pkp3 deficiency causes disruption of an E-cadherin/Rap1 complex required for adherens junction sealing. These findings reveal Pkp3 as a coordinator of desmosome and adherens junction assembly and maturation through its functional association with Rap1.
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