The interaction of nelin, a cardiac-specific ex- pressed protein of human novel gene nelin, with F-actin was studied by both F-actin cosedimentation in vitro and colocal- ization assays. The results showed that nelin ...The interaction of nelin, a cardiac-specific ex- pressed protein of human novel gene nelin, with F-actin was studied by both F-actin cosedimentation in vitro and colocal- ization assays. The results showed that nelin is a new F-actin binding protein and is colocolized with F-actin in cytoplasm of cells. Three new nelin binding proteins, filamin C subtype, titin N2B subtype and inter-alpha trypsin inhibitor heavy chain precursor (ITIH), were identified from human heart cDNA library using yeast two-hybrid screening. The binding activity of filamin C with nelin was confirmed by coim- munoprecipitation. Filamin C binds to nelin through its C-terminal region. It is indicated that nelin is a cytoskeleton associated protein and acts as a membrane-cytoskeleton as- sociated protein involved in the formation of focal adhesions.展开更多
文摘The interaction of nelin, a cardiac-specific ex- pressed protein of human novel gene nelin, with F-actin was studied by both F-actin cosedimentation in vitro and colocal- ization assays. The results showed that nelin is a new F-actin binding protein and is colocolized with F-actin in cytoplasm of cells. Three new nelin binding proteins, filamin C subtype, titin N2B subtype and inter-alpha trypsin inhibitor heavy chain precursor (ITIH), were identified from human heart cDNA library using yeast two-hybrid screening. The binding activity of filamin C with nelin was confirmed by coim- munoprecipitation. Filamin C binds to nelin through its C-terminal region. It is indicated that nelin is a cytoskeleton associated protein and acts as a membrane-cytoskeleton as- sociated protein involved in the formation of focal adhesions.
