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Volumn 582, Issue 5, 2008, Pages 792-798

Putative alternative trans-splicing of leukocyte adhesion-GPCR pre-mRNAs generates functional chimeric receptors

Author keywords

Adhesion GPCR; Alternative splicing; EGF TM7; LNB TM7; trans Splicing

Indexed keywords

CD97 ANTIGEN; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; MEMBRANE PROTEIN;

EID: 39649121700     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.02.004     Document Type: Article
Times cited : (4)

References (50)
  • 1
    • 0034685577 scopus 로고    scopus 로고
    • Human genome project. And the gene number is?
    • Pennisi E. Human genome project. And the gene number is?. Science 288 (2000) 1146-1147
    • (2000) Science , vol.288 , pp. 1146-1147
    • Pennisi, E.1
  • 2
    • 21044431735 scopus 로고    scopus 로고
    • Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution
    • Cheng J., et al. Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution. Science 308 (2005) 1149-1154
    • (2005) Science , vol.308 , pp. 1149-1154
    • Cheng, J.1
  • 3
    • 0034721644 scopus 로고    scopus 로고
    • Protein diversity from alternative splicing: a challenge for bioinformatics and post-genome biology
    • Black D.L. Protein diversity from alternative splicing: a challenge for bioinformatics and post-genome biology. Cell 103 (2000) 367-370
    • (2000) Cell , vol.103 , pp. 367-370
    • Black, D.L.1
  • 4
    • 0035252410 scopus 로고    scopus 로고
    • Alternative splicing: increasing diversity in the proteomic world
    • Graveley B.R. Alternative splicing: increasing diversity in the proteomic world. Trends Genet. 17 (2001) 100-107
    • (2001) Trends Genet. , vol.17 , pp. 100-107
    • Graveley, B.R.1
  • 5
    • 0037062982 scopus 로고    scopus 로고
    • Alternative pre-mRNA splicing and proteome expansion in metazoans
    • Maniatis T., and Tasic B. Alternative pre-mRNA splicing and proteome expansion in metazoans. Nature 418 (2002) 236-243
    • (2002) Nature , vol.418 , pp. 236-243
    • Maniatis, T.1    Tasic, B.2
  • 6
    • 0036337915 scopus 로고    scopus 로고
    • A genomic view of alternative splicing
    • Modrek B., and Lee C. A genomic view of alternative splicing. Nat. Genet. 30 (2002) 13-19
    • (2002) Nat. Genet. , vol.30 , pp. 13-19
    • Modrek, B.1    Lee, C.2
  • 7
    • 0035106880 scopus 로고    scopus 로고
    • Piecing together the significance of splicing
    • Sorek R., and Amitai M. Piecing together the significance of splicing. Nat. Biotechnol. 19 (2001) 196
    • (2001) Nat. Biotechnol. , vol.19 , pp. 196
    • Sorek, R.1    Amitai, M.2
  • 8
    • 32544451144 scopus 로고    scopus 로고
    • Alternative trans-splicing: a novel mode of pre-mRNA processing
    • Horiuchi T., and Aigaki T. Alternative trans-splicing: a novel mode of pre-mRNA processing. Biol. Cell 98 (2006) 135-140
    • (2006) Biol. Cell , vol.98 , pp. 135-140
    • Horiuchi, T.1    Aigaki, T.2
  • 9
    • 0035576933 scopus 로고    scopus 로고
    • Evolutionary origin of SL-addition trans-splicing: still an enigma
    • Nilsen T.W. Evolutionary origin of SL-addition trans-splicing: still an enigma. Trends Genet. 17 (2001) 678-680
    • (2001) Trends Genet. , vol.17 , pp. 678-680
    • Nilsen, T.W.1
  • 10
    • 0028965514 scopus 로고
    • Trans-splicing and polycistronic transcription in Caenorhabditis elegans
    • Blumenthal T. Trans-splicing and polycistronic transcription in Caenorhabditis elegans. Trends Genet. 11 (1995) 132-136
    • (1995) Trends Genet. , vol.11 , pp. 132-136
    • Blumenthal, T.1
  • 11
    • 0037871901 scopus 로고    scopus 로고
    • The modifier of mdg4 locus in Drosophila: functional complexity is resolved by trans splicing
    • Dorn R., and Krauss V. The modifier of mdg4 locus in Drosophila: functional complexity is resolved by trans splicing. Genetica 117 (2003) 165-177
    • (2003) Genetica , vol.117 , pp. 165-177
    • Dorn, R.1    Krauss, V.2
  • 12
    • 0035859961 scopus 로고    scopus 로고
    • Transgene analysis proves mRNA trans-splicing at the complex mod(mdg4) locus in Drosophila
    • Dorn R., Reuter G., and Loewendorf A. Transgene analysis proves mRNA trans-splicing at the complex mod(mdg4) locus in Drosophila. Proc. Natl. Acad. Sci. USA 98 (2001) 9724-9729
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9724-9729
    • Dorn, R.1    Reuter, G.2    Loewendorf, A.3
  • 13
    • 0041358544 scopus 로고    scopus 로고
    • Alternative splicing of lola generates 19 transcription factors controlling axon guidance in Drosophila
    • Goeke S., Greene E.A., Grant P.K., Gates M.A., Crowner D., Aigaki T., and Giniger E. Alternative splicing of lola generates 19 transcription factors controlling axon guidance in Drosophila. Nat. Neurosci. 6 (2003) 917-924
    • (2003) Nat. Neurosci. , vol.6 , pp. 917-924
    • Goeke, S.1    Greene, E.A.2    Grant, P.K.3    Gates, M.A.4    Crowner, D.5    Aigaki, T.6    Giniger, E.7
  • 14
    • 0142027944 scopus 로고    scopus 로고
    • Alternative trans-splicing of constant and variable exons of a Drosophila axon guidance gene, lola
    • Horiuchi T., Giniger E., and Aigaki T. Alternative trans-splicing of constant and variable exons of a Drosophila axon guidance gene, lola. Genes Dev. 17 (2003) 2496-2501
    • (2003) Genes Dev. , vol.17 , pp. 2496-2501
    • Horiuchi, T.1    Giniger, E.2    Aigaki, T.3
  • 15
    • 0029022697 scopus 로고
    • Experimental evidence for RNA trans-splicing in mammalian cells
    • Eul J., Graessmann M., and Graessmann A. Experimental evidence for RNA trans-splicing in mammalian cells. Embo J. 14 (1995) 3226-3235
    • (1995) Embo J. , vol.14 , pp. 3226-3235
    • Eul, J.1    Graessmann, M.2    Graessmann, A.3
  • 16
    • 0022376562 scopus 로고
    • Trans splicing of mRNA precursors in vitro
    • Konarska M.M., Padgett R.A., and Sharp P.A. Trans splicing of mRNA precursors in vitro. Cell 42 (1985) 165-171
    • (1985) Cell , vol.42 , pp. 165-171
    • Konarska, M.M.1    Padgett, R.A.2    Sharp, P.A.3
  • 17
    • 0022386757 scopus 로고
    • Trans splicing of mRNA precursors
    • Solnick D. Trans splicing of mRNA precursors. Cell 42 (1985) 157-164
    • (1985) Cell , vol.42 , pp. 157-164
    • Solnick, D.1
  • 18
    • 0035798105 scopus 로고    scopus 로고
    • Heterologous HIV-nef mRNA trans-splicing: a new principle how mammalian cells generate hybrid mRNA and protein molecules
    • Caudevilla C., Da Silva-Azevedo L., Berg B., Guhl E., Graessmann M., and Graessmann A. Heterologous HIV-nef mRNA trans-splicing: a new principle how mammalian cells generate hybrid mRNA and protein molecules. FEBS Lett. 507 (2001) 269-279
    • (2001) FEBS Lett. , vol.507 , pp. 269-279
    • Caudevilla, C.1    Da Silva-Azevedo, L.2    Berg, B.3    Guhl, E.4    Graessmann, M.5    Graessmann, A.6
  • 21
    • 0033033465 scopus 로고    scopus 로고
    • Trans-splicing of a voltage-gated sodium channel is regulated by nerve growth factor
    • Akopian A.N., Okuse K., Souslova V., England S., Ogata N., and Wood J.N. Trans-splicing of a voltage-gated sodium channel is regulated by nerve growth factor. FEBS Lett. 445 (1999) 177-182
    • (1999) FEBS Lett. , vol.445 , pp. 177-182
    • Akopian, A.N.1    Okuse, K.2    Souslova, V.3    England, S.4    Ogata, N.5    Wood, J.N.6
  • 22
    • 0037135521 scopus 로고    scopus 로고
    • Natural trans-spliced mRNAs are generated from the human estrogen receptor-alpha (hER alpha) gene
    • Flouriot G., Brand H., Seraphin B., and Gannon F. Natural trans-spliced mRNAs are generated from the human estrogen receptor-alpha (hER alpha) gene. J. Biol. Chem. 277 (2002) 26244-26251
    • (2002) J. Biol. Chem. , vol.277 , pp. 26244-26251
    • Flouriot, G.1    Brand, H.2    Seraphin, B.3    Gannon, F.4
  • 23
    • 0037155267 scopus 로고    scopus 로고
    • Intergenic mRNA molecules resulting from trans-splicing
    • Finta C., and Zaphiropoulos P.G. Intergenic mRNA molecules resulting from trans-splicing. J. Biol. Chem. 277 (2002) 5882-5890
    • (2002) J. Biol. Chem. , vol.277 , pp. 5882-5890
    • Finta, C.1    Zaphiropoulos, P.G.2
  • 24
    • 0033574524 scopus 로고    scopus 로고
    • Human acyl-CoA:cholesterol acyltransferase-1 (ACAT-1) gene organization and evidence that the 4.3-kilobase ACAT-1 mRNA is produced from two different chromosomes
    • Li B.L., et al. Human acyl-CoA:cholesterol acyltransferase-1 (ACAT-1) gene organization and evidence that the 4.3-kilobase ACAT-1 mRNA is produced from two different chromosomes. J. Biol. Chem. 274 (1999) 11060-11071
    • (1999) J. Biol. Chem. , vol.274 , pp. 11060-11071
    • Li, B.L.1
  • 25
    • 18444371112 scopus 로고    scopus 로고
    • Promoter choice determines splice site selection in protocadherin alpha and gamma pre-mRNA splicing
    • Tasic B., et al. Promoter choice determines splice site selection in protocadherin alpha and gamma pre-mRNA splicing. Mol. Cell 10 (2002) 21-33
    • (2002) Mol. Cell , vol.10 , pp. 21-33
    • Tasic, B.1
  • 26
  • 27
    • 34547117851 scopus 로고    scopus 로고
    • Restoration of SMN function: delivery of a trans-splicing RNA re-directs SMN2 pre-mRNA splicing
    • Coady T.H., Shababi M., Tullis G.E., and Lorson C.L. Restoration of SMN function: delivery of a trans-splicing RNA re-directs SMN2 pre-mRNA splicing. Mol. Ther. 15 (2007) 1471-1478
    • (2007) Mol. Ther. , vol.15 , pp. 1471-1478
    • Coady, T.H.1    Shababi, M.2    Tullis, G.E.3    Lorson, C.L.4
  • 28
    • 34347330301 scopus 로고    scopus 로고
    • Modulating the expression of disease genes with RNA-based therapy
    • Wood M., Yin H., and McClorey G. Modulating the expression of disease genes with RNA-based therapy. PLoS Genet. 3 (2007) e109
    • (2007) PLoS Genet. , vol.3
    • Wood, M.1    Yin, H.2    McClorey, G.3
  • 29
    • 0029967194 scopus 로고    scopus 로고
    • EGF-TM7: a novel subfamily of seven-transmembrane-region leukocyte cell-surface molecules
    • McKnight A.J., and Gordon S. EGF-TM7: a novel subfamily of seven-transmembrane-region leukocyte cell-surface molecules. Immunol. Today 17 (1996) 283-287
    • (1996) Immunol. Today , vol.17 , pp. 283-287
    • McKnight, A.J.1    Gordon, S.2
  • 30
    • 0031906906 scopus 로고    scopus 로고
    • The EGF-TM7 family: unusual structures at the leukocyte surface
    • McKnight A.J., and Gordon S. The EGF-TM7 family: unusual structures at the leukocyte surface. J. Leukoc. Biol. 63 (1998) 271-280
    • (1998) J. Leukoc. Biol. , vol.63 , pp. 271-280
    • McKnight, A.J.1    Gordon, S.2
  • 32
    • 0034213071 scopus 로고    scopus 로고
    • LNB-TM7, a group of seven-transmembrane proteins related to family-B G-protein-coupled receptors
    • Stacey M., Lin H.H., Gordon S., and McKnight A.J. LNB-TM7, a group of seven-transmembrane proteins related to family-B G-protein-coupled receptors. Trends Biochem. Sci. 25 (2000) 284-289
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 284-289
    • Stacey, M.1    Lin, H.H.2    Gordon, S.3    McKnight, A.J.4
  • 34
    • 0029968118 scopus 로고    scopus 로고
    • Structure of the human CD97 gene: exon shuffling has generated a new type of seven-span transmembrane molecule related to the secretin receptor superfamily
    • Hamann J., Hartmann E., and van Lier R.A. Structure of the human CD97 gene: exon shuffling has generated a new type of seven-span transmembrane molecule related to the secretin receptor superfamily. Genomics 32 (1996) 144-147
    • (1996) Genomics , vol.32 , pp. 144-147
    • Hamann, J.1    Hartmann, E.2    van Lier, R.A.3
  • 35
    • 33845627662 scopus 로고    scopus 로고
    • An unusual mode of concerted evolution of the EGF-TM7 receptor chimera EMR2
    • Kwakkenbos M.J., et al. An unusual mode of concerted evolution of the EGF-TM7 receptor chimera EMR2. Faseb J. 20 (2006) 2582-2584
    • (2006) Faseb J. , vol.20 , pp. 2582-2584
    • Kwakkenbos, M.J.1
  • 36
    • 0034661226 scopus 로고    scopus 로고
    • Human EMR2, a novel EGF-TM7 molecule on chromosome 19p13.1, is closely related to CD97
    • Lin H.H., Stacey M., Hamann J., Gordon S., and McKnight A.J. Human EMR2, a novel EGF-TM7 molecule on chromosome 19p13.1, is closely related to CD97. Genomics 67 (2000) 188-200
    • (2000) Genomics , vol.67 , pp. 188-200
    • Lin, H.H.1    Stacey, M.2    Hamann, J.3    Gordon, S.4    McKnight, A.J.5
  • 37
    • 0030589320 scopus 로고    scopus 로고
    • CD97 is a processed, seven-transmembrane, heterodimeric receptor associated with inflammation
    • Gray J.X., et al. CD97 is a processed, seven-transmembrane, heterodimeric receptor associated with inflammation. J. Immunol. 157 (1996) 5438-5447
    • (1996) J. Immunol. , vol.157 , pp. 5438-5447
    • Gray, J.X.1
  • 38
    • 0029133126 scopus 로고
    • Expression cloning and chromosomal mapping of the leukocyte activation antigen CD97, a new seven-span transmembrane molecule of the secretion receptor superfamily with an unusual extracellular domain
    • Hamann J., et al. Expression cloning and chromosomal mapping of the leukocyte activation antigen CD97, a new seven-span transmembrane molecule of the secretion receptor superfamily with an unusual extracellular domain. J. Immunol. 155 (1995) 1942-1950
    • (1995) J. Immunol. , vol.155 , pp. 1942-1950
    • Hamann, J.1
  • 39
    • 0031922202 scopus 로고    scopus 로고
    • Characterization of the CD55 (DAF)-binding site on the seven-span transmembrane receptor CD97
    • Hamann J., Stortelers C., Kiss-Toth E., Vogel B., Eichler W., and van Lier R.A. Characterization of the CD55 (DAF)-binding site on the seven-span transmembrane receptor CD97. Eur. J. Immunol. 28 (1998) 1701-1707
    • (1998) Eur. J. Immunol. , vol.28 , pp. 1701-1707
    • Hamann, J.1    Stortelers, C.2    Kiss-Toth, E.3    Vogel, B.4    Eichler, W.5    van Lier, R.A.6
  • 40
    • 0029787130 scopus 로고    scopus 로고
    • The seven-span transmembrane receptor CD97 has a cellular ligand (CD55, DAF)
    • Hamann J., Vogel B., van Schijndel G.M., and van Lier R.A. The seven-span transmembrane receptor CD97 has a cellular ligand (CD55, DAF). J. Exp. Med. 184 (1996) 1185-1189
    • (1996) J. Exp. Med. , vol.184 , pp. 1185-1189
    • Hamann, J.1    Vogel, B.2    van Schijndel, G.M.3    van Lier, R.A.4
  • 41
    • 0035968317 scopus 로고    scopus 로고
    • Molecular analysis of the epidermal growth factor-like short consensus repeat domain-mediated protein-protein interactions: dissection of the CD97-CD55 complex
    • Lin H.H., et al. Molecular analysis of the epidermal growth factor-like short consensus repeat domain-mediated protein-protein interactions: dissection of the CD97-CD55 complex. J. Biol. Chem. 276 (2001) 24160-24169
    • (2001) J. Biol. Chem. , vol.276 , pp. 24160-24169
    • Lin, H.H.1
  • 42
    • 14644430368 scopus 로고    scopus 로고
    • Expression of the largest CD97 and EMR2 isoforms on leukocytes facilitates a specific interaction with chondroitin sulfate on B cells
    • Kwakkenbos M.J., Pouwels W., Matmati M., Stacey M., Lin H.H., Gordon S., van Lier R.A., and Hamann J. Expression of the largest CD97 and EMR2 isoforms on leukocytes facilitates a specific interaction with chondroitin sulfate on B cells. J. Leukoc. Biol. 77 (2005) 112-119
    • (2005) J. Leukoc. Biol. , vol.77 , pp. 112-119
    • Kwakkenbos, M.J.1    Pouwels, W.2    Matmati, M.3    Stacey, M.4    Lin, H.H.5    Gordon, S.6    van Lier, R.A.7    Hamann, J.8
  • 43
    • 0141923864 scopus 로고    scopus 로고
    • The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans
    • Stacey M., Chang G.W., Davies J.Q., Kwakkenbos M.J., Sanderson R.D., Hamann J., Gordon S., and Lin H.H. The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans. Blood 102 (2003) 2916-2924
    • (2003) Blood , vol.102 , pp. 2916-2924
    • Stacey, M.1    Chang, G.W.2    Davies, J.Q.3    Kwakkenbos, M.J.4    Sanderson, R.D.5    Hamann, J.6    Gordon, S.7    Lin, H.H.8
  • 44
    • 18444409655 scopus 로고    scopus 로고
    • Method for selecting and enriching cells expressing low affinity ligands for cell surface receptors
    • Lin H.H., Stacey M., Chang G.W., Davies J.Q., and Gordon S. Method for selecting and enriching cells expressing low affinity ligands for cell surface receptors. Biotechniques 38 (2005) 696-698
    • (2005) Biotechniques , vol.38 , pp. 696-698
    • Lin, H.H.1    Stacey, M.2    Chang, G.W.3    Davies, J.Q.4    Gordon, S.5
  • 47
    • 0035878676 scopus 로고    scopus 로고
    • Localization of an exonic splicing enhancer responsible for mammalian natural trans-splicing
    • Caudevilla C., et al. Localization of an exonic splicing enhancer responsible for mammalian natural trans-splicing. Nucleic Acids Res. 29 (2001) 3108-3115
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3108-3115
    • Caudevilla, C.1
  • 48
    • 0028118641 scopus 로고
    • Polypurine sequences within a downstream exon function as a splicing enhancer
    • Tanaka K., Watakabe A., and Shimura Y. Polypurine sequences within a downstream exon function as a splicing enhancer. Mol. Cell Biol. 14 (1994) 1347-1354
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1347-1354
    • Tanaka, K.1    Watakabe, A.2    Shimura, Y.3
  • 49
    • 17044429815 scopus 로고    scopus 로고
    • Delay in synthesis of the 3′ splice site promotes trans-splicing of the preceding 5′ splice site
    • Takahara T., Tasic B., Maniatis T., Akanuma H., and Yanagisawa S. Delay in synthesis of the 3′ splice site promotes trans-splicing of the preceding 5′ splice site. Mol. Cell 18 (2005) 245-251
    • (2005) Mol. Cell , vol.18 , pp. 245-251
    • Takahara, T.1    Tasic, B.2    Maniatis, T.3    Akanuma, H.4    Yanagisawa, S.5
  • 50
    • 35348865583 scopus 로고    scopus 로고
    • EMR1, the human homolog of F4/80, is an eosinophil-specific receptor
    • Hamann J., et al. EMR1, the human homolog of F4/80, is an eosinophil-specific receptor. Eur. J. Immunol. 37 (2007) 2797-2802
    • (2007) Eur. J. Immunol. , vol.37 , pp. 2797-2802
    • Hamann, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.