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Gene Review:

Lasp1 - LIM and SH3 protein 1

Rattus norvegicus

Synonyms: LASP-1, LIM and SH3 domain protein 1

Chew, C.S. et al., Spence, H.J. et al., Nakagawa, H. et al., Phillips, G.R. et al.

Phillips, Anderson, Florens, Gudas, Magda, Yates, Colman, Spence, McGarry, Chew, Carragher, Scott-Carragher, Yuan, Croft, Olson, Frame, Ozanne, Chew, Parente, Chen, Chaponnier, Cameron,

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High impact information on Lasp1

We report here that Krp1, the AP-1 up-regulated protein that has a role in pseudopodial elongation in v-Fos-transformed rat fibroblast cells, forms a novel interaction with the nondifferentially expressed actin binding protein Lasp-1 [1].
In this study, we demonstrate that the cAMP-dependent acid secretory agonist, histamine, induces a rapid, sustained rise in parietal cell lasp-1 phosphorylation and this increase in phosphorylation is closely correlated with the acid secretory response [2].
In primary cultures of gastric fibroblasts, lasp-1 was present mainly within the tips of lamellipodia and at the leading edges of membrane ruffles [2].
Agonist-dependent changes in lasp-1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types [2].
Lasp-1 also was not detectable in proximal tubules in the kidney, in gastrointestinal smooth muscle, heart or skeletal muscle [2].

Biological context of Lasp1

Because cAMP is a potent stimulator of parietal cell acid secretion, we have hypothesized that changes in lasp-1 phosphorylation might be involved in the regulation of ion transport-related activities, perhaps by modulating interactions among cytoskeletal and/or vesicle-associated proteins [2].
For example, gastric chief cells, which contain relatively little F-actin and secrete the enzyme, pepsinogen, by regulated exocytosis, do not appear to express lasp-1 [2].
Localisation of fascin, the LIM and SH3 domain protein 1 (lasp-1), and lasp-2 to the bundles suggest their involvement in that organisation; however, their contributions remain unclear [3].

Anatomical context of Lasp1

Actin-binding proteins in a postsynaptic preparation: Lasp-1 is a component of central nervous system synapses and dendritic spines [4].
Lasp-1 is a unique LIM and src homology 3 (SH3) domain-containing protein that was initially identified as a 40 kDa cAMP-dependent phosphoprotein in the HCl-secreting gastric parietal cell [2].

References

AP-1 differentially expressed proteins Krp1 and fibronectin cooperatively enhance Rho-ROCK-independent mesenchymal invasion by altering the function, localization, and activity of nondifferentially expressed proteins. Spence, H.J., McGarry, L., Chew, C.S., Carragher, N.O., Scott-Carragher, L.A., Yuan, Z., Croft, D.R., Olson, M.F., Frame, M., Ozanne, B.W. Mol. Cell. Biol. (2006) [Pubmed]
The LIM and SH3 domain-containing protein, lasp-1, may link the cAMP signaling pathway with dynamic membrane restructuring activities in ion transporting epithelia. Chew, C.S., Parente, J.A., Chen, X., Chaponnier, C., Cameron, R.S. J. Cell. Sci. (2000) [Pubmed]
Short-term retention of actin filament binding proteins on lamellipodial actin bundles. Nakagawa, H., Terasaki, A.G., Suzuki, H., Ohashi, K., Miyamoto, S. FEBS Lett. (2006) [Pubmed]
Actin-binding proteins in a postsynaptic preparation: Lasp-1 is a component of central nervous system synapses and dendritic spines. Phillips, G.R., Anderson, T.R., Florens, L., Gudas, C., Magda, G., Yates, J.R., Colman, D.R. J. Neurosci. Res. (2004) [Pubmed]

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