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

Terasaki, Asako G.; Suzuki, Hiroshi; Nishioka, Tatsuji; Matsuzawa, Eiji; Katsuki, Miho; Nakagawa, Hiroyuki; Miyamoto, Satoru; Ohashi, Kazuyo

doi:10.1016/j.bbrc.2003.11.085

Cited by 38 publications

(74 citation statements)

References 22 publications

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“…We therefore propose that Lasp links Oskar to the actin cytoskeleton and helps to restrict Oskar activity to the posterior pole after its localized translation. Even though we cannot exclude that Lasp also protects Oskar from degradation, the reduced amounts of oskar mRNA and Oskar protein observed in lasp mutants are probably due to the interdependence of oskar Lasp concentrates in actin-rich subcellular regions, including focal adhesions and lamellipodia in migrating cells (Butt et al, 2003;Chew et al, 2002;Schreiber et al, 1998;Terasaki et al, 2004), and motile growth cones of cultured neurons (Phillips et al, 2004). In our study, we have shown that the NEB repeats of Drosophila Lasp bind actin in vitro and that Lasp colocalizes with actin in vivo.…”

Section: Discussionmentioning

confidence: 64%

The actin-binding protein Lasp promotes Oskar accumulation at the posterior pole of theDrosophilaembryo

et al. 2009

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During Drosophila oogenesis, oskar mRNA is transported to the posterior pole of the oocyte, where it is locally translated and induces germ-plasm assembly. Oskar protein recruits all of the components necessary for the establishment of posterior embryonic structures and of the germline. Tight localization of Oskar is essential, as its ectopic expression causes severe patterning defects. Here, we show that the Drosophila homolog of mammalian Lasp1 protein, an actin-binding protein previously implicated in cell migration in vertebrate cell culture, contributes to the accumulation of Oskar protein at the posterior pole of the embryo. The reduced number of primordial germ cells in embryos derived from lasp mutant females can be rescued only with a form of Lasp that is capable of interacting with Oskar, revealing the physiological importance of the Lasp-Oskar interaction.

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Section: Discussionmentioning

confidence: 64%

The actin-binding protein Lasp promotes Oskar accumulation at the posterior pole of theDrosophilaembryo

et al. 2009

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“…Therefore, probably a significant functional overlap exists between myopalladin and palladin in these tissues. Palladin might also interact with newly characterized protein Lasp-2 and Lim-nebulette (Terasaki et al, 2004;Li et al, 2004), which share the conserved SH3 domain.…”

Section: Discussionmentioning

confidence: 99%

Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin

Rachlin

Otey

2006

Journal of Cell Science

138

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Palladin is a recently described phosphoprotein with an important role in cytoskeletal organization. The major palladin isoform (90-92 kDa) binds to three actin-associated proteins (ezrin, VASP and α-actinin), suggesting that palladin functions as a cytoskeletal scaffold. Here, we describe the organization of the palladin gene, which encodes multiple isoforms, including one (140 kDa) with a similar localization pattern to 90 kDa palladin. Overexpression of the 90 kDa or 140 kDa isoforms in COS-7 cells results in rearrangements of the actin cytoskeleton into super-robust bundles and star-like arrays, respectively. Sequence analysis of 140 kDa palladin revealed a conserved binding site for SH3 domains, suggesting that it binds directly to the SH3-domain protein Lasp-1. Binding of 140 kDa palladin, but not 90 kDa palladin, to Lasp-1 was confirmed by yeast two-hybrid and GST-pull-down assays. Isoform-specific siRNA experiments suggested that 140 kDa palladin plays a role in recruiting Lasp-1 to stress fibers. These results add Lasp-1, an actin-binding protein with a crucial role in cell motility, to the growing list of palladin's binding partners, and suggest that 140 kDa palladin has a specialized function in organizing the actin arrays that participate in cell migration and/or cellular contractility.

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“…Nebulin, nebulette, and N-RAP are muscle-specific and are thus unlikely candidates. Lasp-2 (LIM-nebulette) is a potential candidate because both Lasp-1 and Lasp-2 appear to be expressed in similar cellular compartments in the brain (9,38), and LIMnebulette has a similar subcellular distribution in fibroblasts (21); however, we were unable to detect Lasp-2 expression in the gastric mucosa of either wild-type or Lasp-1-null mice. These findings have led us to tentatively conclude that Lasp-2 does not to perform this function.…”

Section: Discussionmentioning

confidence: 65%

“…Lasp-1 is a member of the nebulin protein family, all members of which possess varying numbers of 35-residue nebulin "repeats." In addition to Lasp-1, this family is known to include nebulin (42), nebulette (26), nebulin-related anchoring protein (N-RAP) (25), and LIM-nebulette (Lasp-2) (21,38). Nebulin, nebulette, and N-RAP are muscle-specific and are thus unlikely candidates.…”

Section: Discussionmentioning

confidence: 99%

Targeted disruption of theLasp-1gene is linked to increases in histamine-stimulated gastric HCl secretion

Chew

Chen

Bollag³

et al. 2008

American Journal of Physiology-Gastrointestinal and Liver Physi

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Lasp-1 (LIM and SH3 domain protein 1) is a multidomain actin-binding protein that is differentially expressed within epithelial tissues and brain. In the gastric mucosa, Lasp-1 is highly expressed in the HCl-secreting parietal cell, where it is prominently localized within the F-actin-rich subcellular regions. Histamine-induced elevation of parietal cell [cAMP]i increases Lasp-1 phosphorylation, which is correlated with activation of HCl secretion. To determine whether Lasp-1 is involved in the regulation of HCl secretion in vivo, we generated a murine model with a targeted disruption of the Lasp-1 gene. Lasp-1-null mice had slightly lower body weights but developed normally and had no overt phenotypic abnormalities. Basal HCl secretion was unaffected by loss of Lasp-1, but histamine stimulation induced a more robust acid secretory response in Lasp-1-null mice compared with wild-type littermates. A similar effect of histamine was observed in isolated gastric glands on the basis of measurements of accumulation of the weak base [14C]aminopyrine. In addition, inhibition of the acid secretory response to histamine by H2 receptor blockade with ranitidine proceeded more slowly in glands from Lasp-1-null mice. These findings support the conclusion that Lasp-1 is involved in the regulation of parietal HCl secretion. We speculate that cAMP-dependent phosphorylation of Lasp-1 alters interactions with F-actin and/or endocytic proteins that interact with Lasp-1, thereby regulating the trafficking/activation of the H+, K+-ATPase (proton pump).

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

Cited by 38 publications

References 22 publications

The actin-binding protein Lasp promotes Oskar accumulation at the posterior pole of theDrosophilaembryo

The actin-binding protein Lasp promotes Oskar accumulation at the posterior pole of theDrosophilaembryo

Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin

Targeted disruption of theLasp-1gene is linked to increases in histamine-stimulated gastric HCl secretion

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