View source for LASP1

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{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''LIM and SH3 domain protein 1''' is a [[protein]] that in humans is encoded by the ''LASP1'' [[gene]].<ref name="pmid7490069">{{cite journal |vauthors=Tomasetto C, Regnier C, Moog-Lutz C, Mattei MG, Chenard MP, Lidereau R, Basset P, Rio MC | title = Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17 | journal = Genomics | volume = 28 | issue = 3 | pages = 367–76 |date=Jan 1996 | pmid = 7490069 | doi = 10.1006/geno.1995.1163 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LASP1 LIM and SH3 protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3927}}</ref>
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.<ref name="entrez"/>
==Interactions==
LASP1 has been shown to [[Protein-protein interaction|interact]] with [[Zyxin]].<ref name=pmid15004028>{{cite journal |last=Li |first=Bo |author2=Zhuang Lei |author3=Trueb Beat  |date=May 2004 |title=Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1 |journal=J. Biol. Chem. |volume=279 |issue=19 |pages=20401–10 |location = United States| issn = 0021-9258| pmid = 15004028 |doi = 10.1074/jbc.M310304200 |doi-access=free }}</ref>
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
*{{cite journal   |vauthors=Tomasetto C, Moog-Lutz C, Régnier CH, etal |title=Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains. |journal=FEBS Lett. |volume=373 |issue= 3 |pages= 245–9 |year= 1995 |pmid= 7589475 |doi=10.1016/0014-5793(95)01040-L  |s2cid=648563 |doi-access=free }}
*{{cite journal   |vauthors=Chew CS, Parente JA, Zhou C, etal |title=Lasp-1 is a regulated phosphoprotein within the cAMP signaling pathway in the gastric parietal cell. |journal=Am. J. Physiol. |volume=275 |issue= 1 Pt 1 |pages= C56–67 |year= 1998 |pmid= 9688835 |doi=  10.1152/ajpcell.1998.275.1.C56}}
*{{cite journal   |vauthors=Schreiber V, Moog-Lutz C, Régnier CH, etal |title=Lasp-1, a novel type of actin-binding protein accumulating in cell membrane extensions. |journal=Mol. Med. |volume=4 |issue= 10 |pages= 675–87 |year= 1999 |pmid= 9848085 |doi=  10.1007/BF03401929| pmc=2230251  }}
*{{cite journal   |vauthors=Chew CS, Chen X, Parente JA, etal |title=Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo. |journal=J. Cell Sci. |volume=115 |issue= Pt 24 |pages= 4787–99 |year= 2003 |pmid= 12432067 |doi=10.1242/jcs.00174  |doi-access= |s2cid=18385678 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal   |vauthors=Butt E, Gambaryan S, Göttfert N, etal |title=Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146. |journal=J. Biol. Chem. |volume=278 |issue= 18 |pages= 15601–7 |year= 2003 |pmid= 12571245 |doi= 10.1074/jbc.M209009200 |doi-access=free  }}
*{{cite journal   |vauthors=Gevaert K, Goethals M, Martens L, etal |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 |s2cid=23783563 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |doi-access= free }}
*{{cite journal  |vauthors=Li B, Zhuang L, Trueb B |title=Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1. |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 20401–10 |year= 2004 |pmid= 15004028 |doi= 10.1074/jbc.M310304200 |doi-access= free }}
*{{cite journal   |vauthors=Keicher C, Gambaryan S, Schulze E, etal |title=Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase. |journal=Biochem. Biophys. Res. Commun. |volume=324 |issue= 1 |pages= 308–16 |year= 2004 |pmid= 15465019 |doi= 10.1016/j.bbrc.2004.08.235 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal   |vauthors=Tao WA, Wollscheid B, O'Brien R, etal |title=Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. |journal=Nat. Methods |volume=2 |issue= 8 |pages= 591–8 |year= 2005 |pmid= 16094384 |doi= 10.1038/nmeth776 |s2cid=20475874 }}
*{{cite journal   |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |bibcode=2005Natur.437.1173R |s2cid=4427026 }}
*{{cite journal   |vauthors=Grunewald TG, Kammerer U, Schulze E, etal |title=Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells. |journal=Exp. Cell Res. |volume=312 |issue= 7 |pages= 974–82 |year= 2006 |pmid= 16430883 |doi= 10.1016/j.yexcr.2005.12.016 }}
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{{PDB Gallery|geneid=3927}}
{{gene-17-stub}}