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F11 receptor

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Title: F11 receptor  
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Subject: CASK, CD1A, CD153, CD320, NKG2
Collection: Clusters of Differentiation
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F11 receptor

F11 receptor

PDB rendering based on 1nbq.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; CD321; JAM; JAM1; JAMA; JCAM; KAT; PAM-1
External IDs GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

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]

Contents

  • Interactions 1
  • References 2
  • Further reading 3
  • External links 4

Interactions

F11 receptor has been shown to interact with MLLT4,[4] CASK[4][5] and Tight junction protein 1.[4][6]

References

  1. ^ Ozaki H, Ishii K, Horiuchi H, Arai H, Kawamoto T, Okawa K, Iwamatsu A, Kita T (July 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.  
  2. ^ Naik UP, Ehrlich YH, Kornecki E (September 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.  
  3. ^ a b "Entrez Gene: F11R F11 receptor". 
  4. ^ a b c Ebnet, K; Schulz C U, Meyer Zu Brickwedde M K, Pendl G G, Vestweber D (September 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.  
  5. ^ Martinez-Estrada, O M; Villa A; Breviario F; Orsenigo F; Dejana E; Bazzoni G (March 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.  
  6. ^ 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 (October 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.  

Further reading

  • Muller WA (2003). "Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response.". Trends Immunol. 24 (6): 327–34.  
  • Bazzoni G (2004). "The JAM family of junctional adhesion molecules.". Curr. Opin. Cell Biol. 15 (5): 525–30.  
  • Naik UP, Eckfeld K (2004). "Junctional adhesion molecule 1 (JAM-1).". J. Biol. Regul. Homeost. Agents 17 (4): 341–7.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Barton ES, Forrest JC, Connolly JL, et al. (2001). "Junction adhesion molecule is a receptor for reovirus.". Cell 104 (3): 441–51.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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