LASP1

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

LIM and SH3 domain protein 1 is a protein that in humans is encoded by the LASP1 gene.

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.

Interactions

LASP1 has been shown to interact with Zyxin.

Further reading

• Tomasetto C, Moog-Lutz C, Régnier CH, et al. (1995). "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. doi:10.1016/0014-5793(95)01040-L. PMID 7589475.
• Chew CS, Parente JA, Zhou C, et al. (1998). "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. PMID 9688835.
• Schreiber V, Moog-Lutz C, Régnier CH, et al. (1999). "Lasp-1, a novel type of actin-binding protein accumulating in cell membrane extensions". Mol. Med. 4 (10): 675–87. PMC 2230251. PMID 9848085.
• Chew CS, Chen X, Parente JA, et al. (2003). "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. doi:10.1242/jcs.00174. PMID 12432067.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Butt E, Gambaryan S, Göttfert N, et al. (2003). "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. doi:10.1074/jbc.M209009200. PMID 12571245.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Li B, Zhuang L, Trueb B (2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. 279 (19): 20401–10. doi:10.1074/jbc.M310304200. PMID 15004028.
• Keicher C, Gambaryan S, Schulze E, et al. (2004). "Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase". Biochem. Biophys. Res. Commun. 324 (1): 308–16. doi:10.1016/j.bbrc.2004.08.235. PMID 15465019.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Tao WA, Wollscheid B, O'Brien R, et al. (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nat. Methods. 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Grunewald TG, Kammerer U, Schulze E, et al. (2006). "Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells". Exp. Cell Res. 312 (7): 974–82. doi:10.1016/j.yexcr.2005.12.016. PMID 16430883.