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Full-Text Articles in Medicine and Health Sciences
Patellin1, A Novel Sec14-Like Protein, Localizes To The Cell Plate And Binds Phosphoinositides, T. Peterman, Yamini Ohol, Lisa Mcreynolds, Elizabeth Luna
Patellin1, A Novel Sec14-Like Protein, Localizes To The Cell Plate And Binds Phosphoinositides, T. Peterman, Yamini Ohol, Lisa Mcreynolds, Elizabeth Luna
Elizabeth J. Luna
Membrane trafficking is central to construction of the cell plate during plant cytokinesis. Consequently, a detailed understanding of the process depends on the characterization of molecules that function in the formation, transport, targeting, and fusion of membrane vesicles to the developing plate, as well as those that participate in its consolidation and maturation into a fully functional partition. Here we report the initial biochemical and functional characterization of patellin1 (PATL1), a novel cell-plate-associated protein that is related in sequence to proteins involved in membrane trafficking in other eukaryotes. Analysis of the Arabidopsis genome indicated that PATL1 is one of a …
F-Actin And Myosin Ii Binding Domains In Supervillin, Yu Chen, Norio Takizawa, Jessica Crowley, Sang Oh, Cheryl Gatto, Taketoshi Kambara, Osamu Sato, Xiang-Dong Li, Mitsuo Ikebe, Elizabeth Luna
F-Actin And Myosin Ii Binding Domains In Supervillin, Yu Chen, Norio Takizawa, Jessica Crowley, Sang Oh, Cheryl Gatto, Taketoshi Kambara, Osamu Sato, Xiang-Dong Li, Mitsuo Ikebe, Elizabeth Luna
Elizabeth J. Luna
Detergent-resistant membranes contain signaling and integral membrane proteins that organize cholesterol-rich domains called lipid rafts. A subset of these detergent-resistant membranes (DRM-H) exhibits a higher buoyant density ( approximately 1.16 g/ml) because of association with membrane skeleton proteins, including actin, myosin II, myosin 1G, fodrin, and an actin- and membrane-binding protein called supervillin (Nebl, T., Pestonjamasp, K. N., Leszyk, J. D., Crowley, J. L., Oh, S. W., and Luna, E. J. (2002) J. Biol. Chem. 277, 43399-43409). To characterize interactions among DRM-H cytoskeletal proteins, we investigated the binding partners of the novel supervillin N terminus, specifically amino acids 1-830. We …