F11 receptor

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Identifiers
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External IDs	GeneCards: [1]
Orthologs
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	Wikidata
View/Edit Human

Junctional adhesion molecule A is a protein that in humans is encoded by the F11R gene.^[1]^[2]^[3] It has also been designated as CD321 (cluster of differentiation 321).

Function

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]

Interactions

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

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". Journal of Immunology. 163 (2): 553–7. PMID 10395639.
↑ Naik UP, Ehrlich YH, Kornecki E (Aug 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". The Biochemical Journal. 310 ( Pt 1) (1): 155–62. PMC 1135867. PMID 7646439.
↑ ^3.0 ^3.1 "Entrez Gene: F11R F11 receptor".
↑ ^4.0 ^4.1 ^4.2 Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (Sep 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". The Journal of Biological Chemistry. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.
↑ Martinez-Estrada OM, 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". The Journal of Biological Chemistry. 276 (12): 9291–6. doi:10.1074/jbc.M006991200. PMID 11120739.
↑ Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D (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". Journal of Cell Science. 116 (Pt 19): 3879–91. doi:10.1242/jcs.00704. PMID 12953056.

Muller WA (Jun 2003). "Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response". Trends in Immunology. 24 (6): 327–34. doi:10.1016/S1471-4906(03)00117-0. PMID 12810109.
Bazzoni G (Oct 2003). "The JAM family of junctional adhesion molecules". Current Opinion in Cell Biology. 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)". Journal of Biological Regulators and Homeostatic Agents. 17 (4): 341–7. PMID 15065765.
Kornecki E, Walkowiak B, Naik UP, Ehrlich YH (Jun 1990). "Activation of human platelets by a stimulatory monoclonal antibody". The Journal of Biological Chemistry. 265 (17): 10042–8. PMID 2351647.
Williams LA, Martin-Padura I, Dejana E, Hogg N, Simmons DL (Dec 1999). "Identification and characterisation of human Junctional Adhesion Molecule (JAM)". Molecular Immunology. 36 (17): 1175–88. doi:10.1016/S0161-5890(99)00122-4. PMID 10698320.
Sobocka MB, Sobocki T, Banerjee P, Weiss C, Rushbrook JI, Norin AJ, Hartwig J, Salifu MO, Markell MS, Babinska A, Ehrlich YH, Kornecki E (Apr 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, Reaves TA, Walsh S, Pochet M, Parkos CA (Jul 2000). "Human junction adhesion molecule regulates tight junction resealing in epithelia". Journal of Cell Science. 113 ( Pt 13) (13): 2363–74. PMID 10852816.
Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (Sep 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". The Journal of Biological Chemistry. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.
Bazzoni G, Martinez-Estrada OM, Orsenigo F, Cordenonsi M, Citi S, Dejana E (Jul 2000). "Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin". The Journal of Biological Chemistry. 275 (27): 20520–6. doi:10.1074/jbc.M905251199. PMID 10877843.
Gupta SK, Pillarisetti K, Ohlstein EH (Jul 2000). "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, 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". The Journal of Biological Chemistry. 276 (12): 9291–6. doi:10.1074/jbc.M006991200. PMID 11120739.
Naik UP, Naik MU, Eckfeld K, Martin-DeLeon P, Spychala J (Feb 2001). "Characterization and chromosomal localization of JAM-1, a platelet receptor for a stimulatory monoclonal antibody". Journal of Cell Science. 114 (Pt 3): 539–47. PMID 11171323.
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Barton ES, Forrest JC, Connolly JL, Chappell JD, Liu Y, Schnell FJ, Nusrat A, Parkos CA, Dermody TS (Feb 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, Pepperkok R, Wiemann S (Sep 2000). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Reports. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
Ebnet K, Suzuki A, Horikoshi Y, Hirose T, Meyer Zu Brickwedde MK, Ohno S, Vestweber D (Jul 2001). "The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)". The EMBO Journal. 20 (14): 3738–48. doi:10.1093/emboj/20.14.3738. PMC 125258. PMID 11447115.
Itoh M, Sasaki H, Furuse M, Ozaki H, Kita T, Tsukita S (Aug 2001). "Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions". The Journal of Cell Biology. 154 (3): 491–7. doi:10.1083/jcb.200103047. PMC 2196413. PMID 11489913.
Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S (Jan 2002). "Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule". The Journal of Biological Chemistry. 277 (1): 455–61. doi:10.1074/jbc.M109005200. PMID 11689568.

External links

KDR+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

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

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[pmid10395639-1] 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". Journal of Immunology. 163 (2): 553–7. PMID 10395639.

[pmid7646439-2] Naik UP, Ehrlich YH, Kornecki E (Aug 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". The Biochemical Journal. 310 ( Pt 1) (1): 155–62. PMC 1135867. PMID 7646439.

[entrez-3] 3.0 ^3.1 "Entrez Gene: F11R F11 receptor".

[pmid10856295-4] 4.0 ^4.1 ^4.2 Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (Sep 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". The Journal of Biological Chemistry. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.

[pmid11120739-5] Martinez-Estrada OM, 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". The Journal of Biological Chemistry. 276 (12): 9291–6. doi:10.1074/jbc.M006991200. PMID 11120739.

[pmid12953056-6] Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D (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". Journal of Cell Science. 116 (Pt 19): 3879–91. doi:10.1242/jcs.00704. PMID 12953056.

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v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
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 d 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
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
101-150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
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 CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201-250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251-300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301-350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

F11 receptor

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Function

Interactions

References

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F11 receptor

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References

Further reading

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