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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM- nebulette and Lasp-1.

Zyxin is a versatile component of focal adhesions in eukaryotic cells. Here we describe a novel binding partner of zyxin, which we have named LIM- nebulette. LIM- nebulette is an alternative splice variant of the sarcomeric protein nebulette, which, in contrast to nebulette, is expressed in non-muscle cells. It displays a modular structure with an N-terminal LIM domain, three nebulin-like repeats, and a C-terminal SH3 domain and shows high similarity to another cytoskeletal protein, Lasp-1 ( LIM and SH3 protein-1). Co-precipitation studies and results obtained with the two-hybrid system demonstrate that LIM- nebulette and Lasp-1 interact specifically with zyxin. Moreover, the SH3 domain from LIM- nebulette is both necessary and sufficient for zyxin binding. The SH3 domains from Lasp-1 and nebulin can also interact with zyxin, but the SH3 domains from more distantly related proteins such as vinexin and sorting nexin 9 do not. On the other hand, the binding site in zyxin is situated at the extreme N terminus as shown by site-directed mutagenesis. LIM- nebulette and Lasp-1 use the same linear binding motif. This motif shows some similarity to a class II binding site but does not contain the classical PXXP sequence. LIM- nebulette reveals a subcellular distribution at focal adhesions similar to Lasp-1. Thus, LIM- nebulette, Lasp-1, and zyxin may play an important role in the organization of focal adhesions.[1]


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