Open Access Articles- Top Results for F11 receptor

F11 receptor

SymbolsF11R ; CD321; JAM; JAM1; JAMA; JCAM; KAT; PAM-1
External IDsOMIM605721 MGI1321398 HomoloGene14255 GeneCards: F11R Gene
RNA expression pattern
File:PBB GE F11R 221664 s at tn.png
File:PBB GE F11R 222354 at tn.png
More reference expression data
RefSeq (mRNA)NM_016946NM_172647
RefSeq (protein)NP_058642NP_766235
Location (UCSC)Chr 1:
160.97 – 160.99 Mb
Chr 1:
171.44 – 171.46 Mb
PubMed search[1][2]

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]


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


  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. PMID 10395639. 
  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. PMC 1135867. PMID 7646439. 
  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. ISSN 0021-9258. PMID 10856295. doi:10.1074/jbc.M002363200. 
  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. ISSN 0021-9258. PMID 11120739. doi:10.1074/jbc.M006991200. 
  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. ISSN 0021-9533. PMID 12953056. doi:10.1242/jcs.00704. 

Further reading


External links

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

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