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Biochem Biophys Res Commun ; 313(1): 48-54, 2004 Jan 02.
Article in English | MEDLINE | ID: mdl-14672696

ABSTRACT

From eluates of F-actin affinity chromatography of chicken brain, we identified a novel actin-binding protein (lasp-2) whose gene was predicted in silico. We cloned cDNA of chicken lasp-2 and analyzed its structure, expression, activity, and localization with lasp-1 (LIM and SH3 protein 1), a previously identified actin-binding protein closely related to lasp-2. Chicken lasp-2 showed high homology to mammalian putative lasp-2. Both chicken lasp-1 and chicken lasp-2 have N-terminal LIM domains, C-terminal SH3 domains, and internal nebulin repeats. However, lasp-2 is greatly different from lasp-1 in the sequence between the second nebulin repeat and a SH3 domain, and the region is conserved in chicken, mouse, and human. As expected from its structural similarity to lasp-1, lasp-2 possessed actin-binding activity and localized with actin filament in filopodia of neuroblastoma. In contrast to lasp-1, which is widely distributed in non-muscle tissues, lasp-2 was highly expressed in brain.


Subject(s)
Brain/metabolism , Homeodomain Proteins/biosynthesis , Neoplasm Proteins , src Homology Domains , Actins/metabolism , Adaptor Proteins, Signal Transducing , Amino Acid Sequence , Animals , Cell Line, Tumor , Chickens , Chromatography, Affinity/methods , Cytoskeletal Proteins , Homeodomain Proteins/chemistry , Homeodomain Proteins/genetics , Homeodomain Proteins/metabolism , Humans , Immunoblotting , LIM Domain Proteins , Mice , Microscopy, Fluorescence , Molecular Sequence Data , Precipitin Tests , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Sequence Homology, Amino Acid , Tissue Distribution
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