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Biochem Biophys Res Commun. 2004 Jan 2;313(1):48-54.

A novel LIM and SH3 protein (lasp-2) highly expressing in chicken brain.

Author information

1
Graduate School of Science and Technology, Chiba University, Chiba 263-8522, Japan. saki@mail.ne.jp

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.

PMID:
14672696
DOI:
10.1016/j.bbrc.2003.11.085
[Indexed for MEDLINE]

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