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- Title
Carom: a novel membrane-associated guanylate kinase-interacting protein with two SH3 domains.
- Authors
Ohno, Hideki; Hirabayashi, Susumu; Kansaku, Ai; Yao, Ikuko; Tajima, Makiko; Nishimura, Wataru; Ohnishi, Hirohide; Mashima, Hirosato; Fujita, Toshiro; Omata, Masao; Hata, Yutaka
- Abstract
MAGI-1 and CASK are membrane-associated guanylate kinases of epithelial junctions. MAGI-1 is localized at tight junctions in polarized epithelial cells, whereas CASK is localized along the lateral membranes. We obtained the KIAA0769 gene product through the yeast two-hybrid screening using MAGI-1 as a bait and named it Carom. Carom has a coiled-coil domain in the middle region, and two src homology 3 domains and a PSD-95/Dlg-A/ZO-1 (PDZ)-binding motif in the C-terminal region. Carom binds to the fifth PDZ domain of MAGI-1 and the calmodulin kinase domain of CASK in vitro. MAGI-1 and CASK bind to the distinct sequences in the C-terminal region of Carom, but still compete with each other for Carom binding. The study using a stable transformant of Madine Darby canine kidney (MDCK) cells expressing GFP-Carom revealed that Carom was partially overlapped by MAGI-1 in MDCK cells, which have not yet established mature cell junctions, but became separated from MAGI-1 and colocalized with CASK in polarized cells. Carom was highly resistant to Triton X-100 extractions and recruited CASK to the Triton X-100-insoluble structures. Carom is a binding partner of CASK, which interacts with CASK in polarized epithelial cells and may link it to the cytoskeleton.Oncogene (2003) 22, 8422-8431. doi:10.1038/sj.onc.1206996
- Subjects
PROTEIN kinases; EPITHELIUM; CALMODULIN; CALCIUM-binding proteins; CELLS
- Publication
Oncogene, 2003, Vol 22, Issue 52, p8422
- ISSN
0950-9232
- Publication type
Article
- DOI
10.1038/sj.onc.1206996