PMID:17968983
| Citation |
Zieseniss, A, Terasaki, AG and Gregorio, CC (2008) Lasp-2 expression, localization, and ligand interactions: a new Z-disc scaffolding protein. Cell Motil. Cytoskeleton 65:59-72 |
|---|---|
| Abstract |
The nebulin family of actin-binding proteins plays an important role in actin filament dynamics in a variety of cells including striated muscle. We report here the identification of a new striated muscle Z-disc associated protein: lasp-2 (LIM and SH3 domain protein-2). Lasp-2 is the most recently identified member of the nebulin family. To evaluate the role of lasp-2 in striated muscle, lasp-2 gene expression and localization were studied in chick and mouse tissue, as well as in primary cultures of chick cardiac and skeletal myocytes. Lasp-2 mRNA was detected as early as chick embryonic stage 25 and lasp-2 protein was associated with developing premyofibril structures, Z-discs of mature myofibrils, focal adhesions, and intercalated discs of cultured cardiomyocytes. Expression of GFP-tagged lasp-2 deletion constructs showed that the C-terminal region of lasp-2 is important for its localization in striated muscle cells. Lasp-2 organizes actin filaments into bundles and interacts directly with the Z-disc protein alpha-actinin. These results are consistent with a function of lasp-2 as a scaffolding and actin filament organizing protein within striated muscle Z-discs. |
| Links |
PubMed Online version:10.1002/cm.20244 |
| Keywords |
Actinin/metabolism; Actins/metabolism; Animals; Cells, Cultured; Chick Embryo; Cytoskeletal Proteins/biosynthesis; Cytoskeletal Proteins/genetics; LIM Domain Proteins; Ligands; Mice; Muscle Proteins/biosynthesis; Muscle Proteins/genetics; Muscle Proteins/metabolism; Muscle, Striated/chemistry; Muscle, Striated/metabolism; Myocytes, Cardiac/chemistry; Myocytes, Cardiac/metabolism; Myofibrils/metabolism; Sarcomeres/chemistry; Sarcomeres/metabolism |
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