LASP1

LIM and SH3 protein 1
PDB rendering based on 1zfo.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3I35​
Identifiers
Symbols	LASP1 ; Lasp-1; MLN50
External IDs	OMIM: 602920 MGI: 109656 HomoloGene: 4480 GeneCards: LASP1 Gene
Gene ontology Molecular function • SH3/SH2 adaptor activity • protein binding • zinc ion binding • ion transmembrane transporter activity • actin filament binding Cellular component • focal adhesion • cortical actin cytoskeleton • extracellular exosome Biological process • ion transport • positive regulation of signal transduction • ion transmembrane transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3927	16796
Ensembl	ENSG00000002834	ENSMUSG00000038366
UniProt	Q14847	Q61792
RefSeq (mRNA)	NM_001271608	NM_010688
RefSeq (protein)	NP_001258537	NP_034818
Location (UCSC)	Chr 17: 38.87 – 38.92 Mb	Chr 11: 97.8 – 97.84 Mb
PubMed search

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]

References

1. Tomasetto C, Regnier C, Moog-Lutz C, Mattei MG, Chenard MP, Lidereau R, Basset P, Rio MC (Jan 1996). "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. doi:10.1006/geno.1995.1163. PMID 7490069.
2. "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. (United States) 279 (19): 20401–10. doi:10.1074/jbc.M310304200. ISSN 0021-9258. PMID 15004028.

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.