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Gene Review

LASP1  -  LIM and SH3 protein 1

Homo sapiens

Synonyms: LASP-1, LIM and SH3 domain protein 1, Lasp-1, MLN 50, MLN50, ...
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Disease relevance of LASP1


High impact information on LASP1

  • Cotransfection of PtK-2 cells with LASP and cGK confirmed phosphorylation of LASP in vivo [4].
  • Taken together, these data suggest that phosphorylation of LASP by cGK and cAK may be involved in cytoskeletal organization and cell motility [4].
  • In the present study we identified the LIM and SH3 domain protein (LASP) that was recently cloned from human breast cancer cells (Tomasetto, C., Regnier, C., Moog-Lutz, C., Mattei, M. G., Chenard, M. P., Liderau, R., Basset, P., and Rio, M. C. (1995) Genomics 28, 367-376) as a novel substrate of cGK in human platelets [4].
  • LASP is an actin-binding protein, and the phospho-LASP-mimicking mutant S146D showed reduced binding affinity for F-actin in cosedimentation experiments [4].
  • Studies with human LASP mutants identified serine 146 as a specific phosphorylation site for cGK and cAK in vivo [4].

Biological context of LASP1

  • Here, we identified and characterized a novel LASP1-related gene, LASP2, by using bioinformatics [5].
  • The LASP1 gene was localized to a pair of microchromosomes and the LASP2 gene was localized to chromosome 2p3.1, indicating that the chromosomal locations of the LASP1 and LASP2 genes are highly conserved between chicken and human [6].
  • Our results have yielded many novel and interesting genes exhibiting differential expression in lactating mammary tissue, including oncogenes (VAV3, C-myc), mediators of apoptosis (Caspase 8), and cell cycle regulators (LASP1) [7].
  • Microsequencing and site-directed mutagenesis localized the major in vivo and in vitro PKA-dependent phosphorylation sites in rabbit lasp-1 to S(99) and S(146) [8].
  • Transfection of lasp-1 cDNA encoding for alanine substitutions at S(99) and S(146), into parietal cells appeared to suppress the cAMP-dependent translocation of lasp-1 to the intracellular canalicular region [8].

Anatomical context of LASP1

  • The localization of lasp-1 to these subcellular regions under a range of experimental conditions and the phosphorylation-dependent regulation of this protein in F-actin rich epithelial cells suggests an integral and possibly cell-specific role in modulating cytoskeletal/membrane-based cellular activities [8].
  • In gastric fibroblasts, exposure to the protein kinase C activator, PMA, was correlated with the translocation of lasp-1 into newly formed F-actin-rich lamellipodial extensions and nascent focal complexes [8].
  • In the gastric parietal cell, cAMP-dependent phosphorylation induces the partial translocation of lasp-1 to the apically directed F-actin-rich canalicular membrane, which is the site of active HCl secretion [8].
  • In addition, we provide evidence that lasp-1 is concentrated within focal complexes as well as in the leading edges of lamellipodia and the tips of filopodia in non-transformed gastric fibroblasts [8].
  • Lasp-1 has been identified as a signaling molecule that is phosphorylated upon elevation of [cAMP]i in pancreas, intestine and gastric mucosa and is selectively expressed in cells within epithelial tissues [8].

Associations of LASP1 with chemical compounds

  • LASP2 and LASP1 were the LASP family proteins consisting of LIM domain, Nebulin repeat, and SH3 domain [5].
  • Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase [9].

Physical interactions of LASP1


Other interactions of LASP1


Analytical, diagnostic and therapeutic context of LASP1

  • We determined the chromosomal locations of the LASP1 and LASP2 genes in chicken by fluorescence in situ hybridization [6].
  • Immunoblotting of LASP-1 in various mouse and human tissues detected a similar prominent expression in non-muscle tissue [9].
  • Combined Northern and Western blot analyses indicate that pp40/lasp-1 is widely expressed (through a single 3.3-kb message) not only in epithelial tissues but also in muscle and brain [12].


  1. The human LASP1 gene is fused to MLL in an acute myeloid leukemia with t(11;17)(q23;q21). Strehl, S., Borkhardt, A., Slany, R., Fuchs, U.E., König, M., Haas, O.A. Oncogene (2003) [Pubmed]
  2. Overexpression of LASP-1 mediates migration and proliferation of human ovarian cancer cells and influences zyxin localisation. Grunewald, T.G., Kammerer, U., Winkler, C., Schindler, D., Sickmann, A., Honig, A., Butt, E. Br. J. Cancer (2007) [Pubmed]
  3. Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains. Tomasetto, C., Moog-Lutz, C., Régnier, C.H., Schreiber, V., Basset, P., Rio, M.C. FEBS Lett. (1995) [Pubmed]
  4. Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146. Butt, E., Gambaryan, S., Göttfert, N., Galler, A., Marcus, K., Meyer, H.E. J. Biol. Chem. (2003) [Pubmed]
  5. Identification and characterization of LASP2 gene in silico. Katoh, M., Katoh, M. Int. J. Mol. Med. (2003) [Pubmed]
  6. Chromosomal assignment of LASP1 and LASP2 genes and organization of the LASP2 gene in chicken. Terasaki, A.G., Suzuki, H., Ando, J., Matsuda, Y., Ohashi, K. Cytogenet. Genome Res. (2006) [Pubmed]
  7. Bovine mammary gene expression profiling using a cDNA microarray enhanced for mammary-specific transcripts. Suchyta, S.P., Sipkovsky, S., Halgren, R.G., Kruska, R., Elftman, M., Weber-Nielsen, M., Vandehaar, M.J., Xiao, L., Tempelman, R.J., Coussens, P.M. Physiol. Genomics (2003) [Pubmed]
  8. Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo. Chew, C.S., Chen, X., Parente, J.A., Tarrer, S., Okamoto, C., Qin, H.Y. J. Cell. Sci. (2002) [Pubmed]
  9. Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase. Keicher, C., Gambaryan, S., Schulze, E., Marcus, K., Meyer, H.E., Butt, E. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  10. Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells. Grunewald, T.G., Kammerer, U., Schulze, E., Schindler, D., Honig, A., Zimmer, M., Butt, E. Exp. Cell Res. (2006) [Pubmed]
  11. Linker region of nebulin family members plays an important role in targeting these molecules to cellular structures. Panaviene, Z., Moncman, C.L. Cell Tissue Res. (2007) [Pubmed]
  12. Lasp-1 is a regulated phosphoprotein within the cAMP signaling pathway in the gastric parietal cell. Chew, C.S., Parente, J.A., Zhou, C., Baranco, E., Chen, X. Am. J. Physiol. (1998) [Pubmed]
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