大野　秀樹    Department   School of Medicine(Tokyo Women's Medical University Adachi Medical Center), School of Medicine    Position   Assistant Professor
Article types	Original article
Language	English
Peer review	Peer reviewed
Title	Carom: a novel membrane-associated guanylate kinase-interacting protein with two SH3 domains
Journal	Formal name：Oncogene ISSN code：0950-9232 (Print) 0950-9232 (Linking)
Domestic / Foregin	Foregin
Volume, Issue, Page	22,pp.8422-31
Author and coauthor	Ohno, H., Hirabayashi, S., Kansaku, A., Yao, I., Tajima, M., Nishimura, W., Ohnishi, H., Mashima, H., Fujita, T., Omata, M., Hata, Y.
Authorship	Lead author
Publication date	2003
Summary	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.
DOI	10.1038/sj.onc.1206996
Document No.	14627983