3mj7

Structural highlights

Function

[JAML1_MOUSE] Transmembrane protein of the plasma membrane of leukocytes that control their migration and activation through interaction with CXADR, a plasma membrane receptor found on adjacent epithelial and endothelial cells. The interaction between both receptors mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, AMICA1 induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair. It also controls the transmigration of leukocytes within epithelial and endothelial tissues through adhesive interactions with epithelial and endothelial CXADR.^[1] [CXAR_MOUSE] Component of the epithelial apical junction complex that is essential for the tight junction integrity. Proposed to function as a homophilic cell adhesion molecule. Recruits MPDZ to intercellular contact sites. Probably involved in transepithelial migration of polymorphonuclear leukocytes (PMN) through adhesive interactions with AMICA1/JAML located in the plasma membrane of PMN (By similarity).^{[2] [3] [4]} In vitro, acts as a receptor for group B coxsackieviruses and subgroup C of adenoviruses (AD2 and AD5).^{[5] [6] [7]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

1. ↑ Witherden DA, Verdino P, Rieder SE, Garijo O, Mills RE, Teyton L, Fischer WH, Wilson IA, Havran WL. The junctional adhesion molecule JAML is a costimulatory receptor for epithelial gammadelta T cell activation. Science. 2010 Sep 3;329(5996):1205-10. PMID:20813954 doi:10.1126/science.1192698
2. ↑ Bergelson JM, Cunningham JA, Droguett G, Kurt-Jones EA, Krithivas A, Hong JS, Horwitz MS, Crowell RL, Finberg RW. Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5. Science. 1997 Feb 28;275(5304):1320-3. PMID:9036860
3. ↑ Bergelson JM, Krithivas A, Celi L, Droguett G, Horwitz MS, Wickham T, Crowell RL, Finberg RW. The murine CAR homolog is a receptor for coxsackie B viruses and adenoviruses. J Virol. 1998 Jan;72(1):415-9. PMID:9420240
4. ↑ Honda T, Saitoh H, Masuko M, Katagiri-Abe T, Tominaga K, Kozakai I, Kobayashi K, Kumanishi T, Watanabe YG, Odani S, Kuwano R. The coxsackievirus-adenovirus receptor protein as a cell adhesion molecule in the developing mouse brain. Brain Res Mol Brain Res. 2000 Apr 14;77(1):19-28. PMID:10814828
5. ↑ Bergelson JM, Cunningham JA, Droguett G, Kurt-Jones EA, Krithivas A, Hong JS, Horwitz MS, Crowell RL, Finberg RW. Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5. Science. 1997 Feb 28;275(5304):1320-3. PMID:9036860
6. ↑ Bergelson JM, Krithivas A, Celi L, Droguett G, Horwitz MS, Wickham T, Crowell RL, Finberg RW. The murine CAR homolog is a receptor for coxsackie B viruses and adenoviruses. J Virol. 1998 Jan;72(1):415-9. PMID:9420240
7. ↑ Honda T, Saitoh H, Masuko M, Katagiri-Abe T, Tominaga K, Kozakai I, Kobayashi K, Kumanishi T, Watanabe YG, Odani S, Kuwano R. The coxsackievirus-adenovirus receptor protein as a cell adhesion molecule in the developing mouse brain. Brain Res Mol Brain Res. 2000 Apr 14;77(1):19-28. PMID:10814828
8. ↑ Verdino P, Witherden DA, Havran WL, Wilson IA. The molecular interaction of CAR and JAML recruits the central cell signal transducer PI3K. Science. 2010 Sep 3;329(5996):1210-4. PMID:20813955 doi:10.1126/science.1187996