Erratum to “Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells” [Exp. Cell Res. 312 (2006) 974–982]

LIM and SH3 protein 1 (Lasp1) is a novel p53 transcriptional target involved in hepatocellular carcinoma

“…These results indicate that depletion of Lasp1 by siRNA suppresses the cell migratory and invasive ability, suggesting that HCC cells may acquire higher metastasis potential by over-expressing Lasp1. Consistent with several previous reports [11,20], further overexpression of Lasp1 in these three HCC cell lines also significantly inhibited cell migratory and invasive activity (Table 1). These results support the conclusion that Lasp1 plays important roles in regulating cell motility.…”

“…Alterations in Lasp1 levels can also have an impact on cell growth as suggested by previous studies in breast and ovarian cancer [10,11]. In our hands, depletion of Lasp1 by specific siRNA inhibited HCC cell proliferation in both monolayer and anchorage-independent growth in soft agar, while over-expression of Lasp1 significantly enhanced cell proliferation (Fig.…”

“…The results suggest that the normal cytoskeleton structure and cell motility are dependent upon the intracellular level of Lasp1. One possible explanation for the observed effect of reduced cell motility with excess Lasp1 is the disruption of cytoskeleton structure [11], while depletion of Lasp1 may cause cellular localization change of its binding partners at the focal adhesion site as it functions as a scaffolding protein. This is in agreement with the proposed role of Lasp1 as a recruiting protein for zyxin [31].…”

“…Silencing of Lasp1 by siRNA suppressed cell proliferation and migration of breast cancer cells [11] and a similar approach using ovarian cancer cells further substantiated its functional role by arresting cells at G2/M phase, reducing cell proliferation and affecting zyxin localization [10]. The human Lasp1 gene encodes a protein of 261 amino acids containing an N-terminal LIM domain followed by two actin binding sites and a C-terminal src homology SH3 domain [12].…”