F11 receptor
From Wikipedia, the free encyclopedia
Junctional adhesion molecule A is a protein that in humans is encoded by the F11R gene.[1][2][3] KDR has also been designated as CD321 (cluster of differentiation 321).
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple transcript variants encoding two different isoforms have been found for this gene.[3]
[edit] Interactions
F11 receptor has been shown to interact with MLLT4,[4] CASK[5][4] and Tight junction protein 1.[4][6]
[edit] References
- ^ Ozaki H, Ishii K, Horiuchi H, Arai H, Kawamoto T, Okawa K, Iwamatsu A, Kita T (Jul 1999). "Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells". J Immunol 163 (2): 553–7. PMID 10395639.
- ^ Naik UP, Ehrlich YH, Kornecki E (Sep 1995). "Mechanisms of platelet activation by a stimulatory antibody: cross-linking of a novel platelet receptor for monoclonal antibody F11 with the Fc gamma RII receptor". Biochem J 310 (1): 155–62. PMC 1135867. PMID 7646439. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1135867.
- ^ a b "Entrez Gene: F11R F11 receptor". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50848.
- ^ a b c Ebnet, K; Schulz C U, Meyer Zu Brickwedde M K, Pendl G G, Vestweber D (Sep. 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". J. Biol. Chem. (UNITED STATES) 275 (36): 27979–88. doi:10.1074/jbc.M002363200. ISSN 0021-9258. PMID 10856295.
- ^ Martinez-Estrada, O M; Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G (Mar. 2001). "Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells". J. Biol. Chem. (United States) 276 (12): 9291–6. doi:10.1074/jbc.M006991200. ISSN 0021-9258. PMID 11120739.
- ^ Ebnet, Klaus; Aurrand-Lions Michel, Kuhn Annegret, Kiefer Friedemann, Butz Stefan, Zander Kerstin, Meyer zu Brickwedde Maria-Katharina, Suzuki Atsushi, Imhof Beat A, Vestweber Dietmar (Oct. 2003). "The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity". J. Cell. Sci. (England) 116 (Pt 19): 3879–91. doi:10.1242/jcs.00704. ISSN 0021-9533. PMID 12953056.
[edit] Further reading
- Muller WA (2003). "Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response.". Trends Immunol. 24 (6): 327–34. doi:10.1016/S1471-4906(03)00117-0. PMID 12810109.
- Bazzoni G (2004). "The JAM family of junctional adhesion molecules.". Curr. Opin. Cell Biol. 15 (5): 525–30. doi:10.1016/S0955-0674(03)00104-2. PMID 14519386.
- Naik UP, Eckfeld K (2004). "Junctional adhesion molecule 1 (JAM-1).". J. Biol. Regul. Homeost. Agents 17 (4): 341–7. PMID 15065765.
- Kornecki E, Walkowiak B, Naik UP, Ehrlich YH (1990). "Activation of human platelets by a stimulatory monoclonal antibody.". J. Biol. Chem. 265 (17): 10042–8. PMID 2351647.
- Williams LA, Martin-Padura I, Dejana E, et al. (2000). "Identification and characterisation of human Junctional Adhesion Molecule (JAM).". Mol. Immunol. 36 (17): 1175–88. doi:10.1016/S0161-5890(99)00122-4. PMID 10698320.
- Sobocka MB, Sobocki T, Banerjee P, et al. (2000). "Cloning of the human platelet F11 receptor: a cell adhesion molecule member of the immunoglobulin superfamily involved in platelet aggregation.". Blood 95 (8): 2600–9. PMID 10753840.
- Liu Y, Nusrat A, Schnell FJ, et al. (2000). "Human junction adhesion molecule regulates tight junction resealing in epithelia.". J. Cell. Sci. 113 (13): 2363–74. PMID 10852816.
- Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, et al. (2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1.". J. Biol. Chem. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.
- Bazzoni G, Martinez-Estrada OM, Orsenigo F, et al. (2000). "Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin.". J. Biol. Chem. 275 (27): 20520–6. doi:10.1074/jbc.M905251199. PMID 10877843.
- Gupta SK, Pillarisetti K, Ohlstein EH (2001). "Platelet agonist F11 receptor is a member of the immunoglobulin superfamily and identical with junctional adhesion molecule (JAM): regulation of expression in human endothelial cells and macrophages.". IUBMB Life 50 (1): 51–6. doi:10.1080/15216540050176593. PMID 11087121.
- Martinez-Estrada OM, Villa A, Breviario F, et al. (2001). "Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells.". J. Biol. Chem. 276 (12): 9291–6. doi:10.1074/jbc.M006991200. PMID 11120739.
- Naik UP, Naik MU, Eckfeld K, et al. (2001). "Characterization and chromosomal localization of JAM-1, a platelet receptor for a stimulatory monoclonal antibody.". J. Cell. Sci. 114 (Pt 3): 539–47. PMID 11171323.
- Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=311072.
- Barton ES, Forrest JC, Connolly JL, et al. (2001). "Junction adhesion molecule is a receptor for reovirus.". Cell 104 (3): 441–51. doi:10.1016/S0092-8674(01)00231-8. PMID 11239401.
- Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing.". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1083732.
- Ebnet K, Suzuki A, Horikoshi Y, et al. (2001). "The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM).". EMBO J. 20 (14): 3738–48. doi:10.1093/emboj/20.14.3738. PMC 125258. PMID 11447115. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125258.
- Itoh M, Sasaki H, Furuse M, et al. (2001). "Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions.". J. Cell Biol. 154 (3): 491–7. doi:10.1083/jcb.200103047. PMC 2196413. PMID 11489913. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2196413.
- Hamazaki Y, Itoh M, Sasaki H, et al. (2002). "Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule.". J. Biol. Chem. 277 (1): 455–61. doi:10.1074/jbc.M109005200. PMID 11689568.
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PDB gallery
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1nbq: Crystal Structure of Human Junctional Adhesion Molecule Type 1
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[edit] External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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| 1-50 |
CD1 ( a-c, 1A, 1D, 1E) · CD2 · CD3 ( γ, δ, ε) · CD4 · CD5 · CD6 · CD7 · CD8 ( a) · CD9 · CD10 · CD11 ( a, b, c) · CD13 · CD14 · CD15 · CD16 ( A, B) · CD18 · CD19 · CD20 · CD21 · CD22 · CD23 · CD24 · CD25 · CD26 · CD27 · CD28 · CD29 · CD30 · CD31 · CD32 ( A, B) · CD33 · CD34 · CD35 · CD36 · CD37 · CD38 · CD39 · CD40 · CD41 · CD42 ( a, b, c, d) · CD43 · CD44 · CD45 · CD46 · CD47 · CD48 · CD49 ( a, b, c, d, e, f) · CD50
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| 51-100 |
CD51 · CD52 · CD53 · CD54 · CD55 · CD56 · CD57 · CD58 · CD59 · CD61 · CD62 ( E, L, P) · CD63 · CD64 ( A, B, C) · CD66 ( a, b, c, d, e, f) · CD68 · CD69 · CD70 · CD71 · CD72 · CD73 · CD74 · CD78 · CD79 ( a, b) · CD80 · CD81 · CD82 · CD83 · CD84 · CD85 ( a, d, e, h, j, k) · CD86 · CD87 · CD88 · CD89 · CD90 · CD91- CD92 · CD93 · CD94 · CD95 · CD96 · CD97 · CD98 · CD99 · CD100
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| 151-200 |
CD151 · CD152 · CD153 · CD154 · CD155 · CD156 ( a, b, c) · CD157 · CD158 ( a, d, e, i, k) · CD159 ( a, c) · CD160 · CD161 · CD162 · CD163 · CD164 · CD166 · CD167 ( a, b) · CD168 · CD169 · CD170 · CD171 · CD172 ( a, b, g) · CD174 · CD177 · CD178 · CD179 ( a, b) · CD181 · CD182 · CD183 · CD184 · CD185 · CD186 · CD191 · CD192 · CD193 · CD194 · CD195 · CD196 · CD197 · CDw198 · CDw199 · CD200
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| 251-300 |
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| 301-350 |
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