LPXN

{{Short description|Protein-coding gene in the species Homo sapiens}}

Leupaxin is a protein that in humans is encoded by the LPXN gene.{{cite journal |vauthors=Lipsky BP, Beals CR, Staunton DE | title = Leupaxin is a novel LIM domain protein that forms a complex with PYK2 | journal = J Biol Chem | volume = 273 | issue = 19 | pages = 11709–13 |date=Jun 1998 | pmid = 9565592 | doi =10.1074/jbc.273.19.11709 | doi-access = free }}{{cite web | title = Entrez Gene: LPXN leupaxin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9404}}

The product encoded by this gene is preferentially expressed in hematopoietic cells and is most homologous to the focal adhesion protein, paxillin. It may function in cell type-specific signaling by associating with PYK2, a member of focal adhesion kinase family. As a substrate for a tyrosine kinase in lymphoid cells, this protein may also function in, and be regulated by tyrosine kinase activity.

References

{{cite journal |vauthors=Chew V, Lam KP |title=Leupaxin negatively regulates B cell receptor signaling. |journal=J. Biol. Chem. |volume=282 |issue= 37 |pages= 27181–91 |year= 2007 |pmid= 17640867 |doi= 10.1074/jbc.M704625200 |doi-access= free }}
{{cite journal |vauthors=Sahu SN, Nunez S, Bai G, Gupta A |title=Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells. |journal=Am. J. Physiol., Cell Physiol. |volume=292 |issue= 6 |pages= C2288–96 |year= 2007 |pmid= 17329398 |doi= 10.1152/ajpcell.00503.2006 }}
{{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=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=Watanabe N, Amano N, Ishizuka H, Mashima K |title=Leupaxin binds to PEST domain tyrosine phosphatase PEP. |journal=Mol. Cell. Biochem. |volume=269 |issue= 1–2 |pages= 13–7 |year= 2005 |pmid= 15786712 |doi=10.1007/s11010-005-2149-6 |s2cid=21854825 }}
{{cite journal |vauthors=Rush J, Moritz A, Lee KA, etal |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94–101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046 |s2cid=7200157 }}
{{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=Brill LM, Salomon AR, Ficarro SB, etal |title=Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. |journal=Anal. Chem. |volume=76 |issue= 10 |pages= 2763–72 |year= 2004 |pmid= 15144186 |doi= 10.1021/ac035352d }}
{{cite journal |vauthors=Gupta A, Lee BS, Khadeer MA, etal |title=Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast. |journal=J. Bone Miner. Res. |volume=18 |issue= 4 |pages= 669–85 |year= 2003 |pmid= 12674328 |doi=10.1359/jbmr.2003.18.4.669 |s2cid=24743841 |doi-access=free }}
{{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=Liu S, Thomas SM, Woodside DG, etal |title=Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses. |journal=Nature |volume=402 |issue= 6762 |pages= 676–81 |year= 2000 |pmid= 10604475 |doi= 10.1038/45264 |s2cid=2770368 }}
{{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
{{cite journal |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}

LPXN

References

Further reading