LASP1 explained

LIM and SH3 domain protein 1 is a protein that in humans is encoded by the LASP1 gene.^{[1] [2]}

This gene encodes a member of a LIM protein subfamily which is characterized by a LIM motif and a domain of Src homology region 3. This protein functions as an actin-binding protein and possibly in cytoskeletal organization.^[2]

Interactions

LASP1 has been shown to interact with Zyxin.^[3]

Further reading

• Tomasetto C, Moog-Lutz C, Régnier CH, etal . Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains. . FEBS Lett. . 373 . 3 . 245–9 . 1995 . 7589475 . 10.1016/0014-5793(95)01040-L . 648563 . free .
• Chew CS, Parente JA, Zhou C, etal . Lasp-1 is a regulated phosphoprotein within the cAMP signaling pathway in the gastric parietal cell. . Am. J. Physiol. . 275 . 1 Pt 1 . C56–67 . 1998 . 9688835 . 10.1152/ajpcell.1998.275.1.C56.
• Schreiber V, Moog-Lutz C, Régnier CH, etal . Lasp-1, a novel type of actin-binding protein accumulating in cell membrane extensions. . Mol. Med. . 4 . 10 . 675–87 . 1999 . 9848085 . 10.1007/BF03401929. 2230251 .
• Chew CS, Chen X, Parente JA, etal . Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo. . J. Cell Sci. . 115 . Pt 24 . 4787–99 . 2003 . 12432067 . 10.1242/jcs.00174 . 18385678 .
• Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Butt E, Gambaryan S, Göttfert N, etal . Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146. . J. Biol. Chem. . 278 . 18 . 15601–7 . 2003 . 12571245 . 10.1074/jbc.M209009200 . free .
• Gevaert K, Goethals M, Martens L, etal . Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. . Nat. Biotechnol. . 21 . 5 . 566–9 . 2004 . 12665801 . 10.1038/nbt810 . 23783563 .
• Ota T, Suzuki Y, Nishikawa T, etal . Complete sequencing and characterization of 21,243 full-length human cDNAs. . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . free .
• Li B, Zhuang L, Trueb B . Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1. . J. Biol. Chem. . 279 . 19 . 20401–10 . 2004 . 15004028 . 10.1074/jbc.M310304200 . free .
• Keicher C, Gambaryan S, Schulze E, etal . Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase. . Biochem. Biophys. Res. Commun. . 324 . 1 . 308–16 . 2004 . 15465019 . 10.1016/j.bbrc.2004.08.235 .
• Gerhard DS, Wagner L, Feingold EA, etal . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
• Tao WA, Wollscheid B, O'Brien R, etal . Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. . Nat. Methods . 2 . 8 . 591–8 . 2005 . 16094384 . 10.1038/nmeth776 . 20475874 .
• Rual JF, Venkatesan K, Hao T, etal . Towards a proteome-scale map of the human protein-protein interaction network. . Nature . 437 . 7062 . 1173–8 . 2005 . 16189514 . 10.1038/nature04209 . 2005Natur.437.1173R . 4427026 .
• Grunewald TG, Kammerer U, Schulze E, etal . Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells. . Exp. Cell Res. . 312 . 7 . 974–82 . 2006 . 16430883 . 10.1016/j.yexcr.2005.12.016 .

Notes and References

1. Tomasetto C, Regnier C, Moog-Lutz C, Mattei MG, Chenard MP, Lidereau R, Basset P, Rio MC . Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17 . Genomics . 28 . 3 . 367–76 . Jan 1996 . 7490069 . 10.1006/geno.1995.1163 .
2. Web site: Entrez Gene: LASP1 LIM and SH3 protein 1.
3. Li . Bo . Zhuang Lei . Trueb Beat . May 2004 . Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1 . J. Biol. Chem. . 279 . 19 . 20401–10 . United States. 0021-9258. 15004028 . 10.1074/jbc.M310304200 . free .