Junctional adhesion molecule

Junctional Adhesion Molecule
Crystallographic structure of junctional adhesion molecules linked together
Identifiers
SymbolJAM
MembranomeImmunoglobulinset domain V set domain

A junctional adhesion molecule (JAM) is a protein that is a member of the immunoglobulin superfamily,[1][2] and is expressed in a variety of different tissues, such as leukocytes, platelets, and epithelial and endothelial cells.[2] They have been shown to regulate signal complex assembly on both their cytoplasmic and extracellular domains through interaction with scaffolding that contains a PDZ domain and adjacent cell's receptors, respectively.[3] JAMs adhere to adjacent cells through interactions with integrins LFA-1 and Mac-1, which are contained in leukocyte β2 and α4β1, which is contained in β1. JAMs have many influences on leukocyte-endothelial cell interactions, which are primarily moderated by the integrins discussed above.[4] They interact in their cytoplasmic domain with scaffold proteins that contain a PDZ domain, which are common protein interaction modules that target short amino acid sequences at the C-terminus of proteins, to form tight junctions in both epithelial and endothelial cells as polarity is gained in the cell.[3]

  1. ^ Greene C, Campbell M, Janigro D (January 2019). "Chapter 1 - Fundamentals of Brain–Barrier Anatomy and Global Functions". In Lonser RR, Sarntinoranont M, Bankiewicz K (eds.). Nervous System Drug Delivery. Academic Press. pp. 3–20. doi:10.1016/b978-0-12-813997-4.00001-3. ISBN 978-0-12-813997-4. S2CID 198273920.
  2. ^ a b Ebnet K, Suzuki A, Ohno S, Vestweber D (January 2004). "Junctional adhesion molecules (JAMs): more molecules with dual functions?". Journal of Cell Science. 117 (Pt 1): 19–29. doi:10.1242/jcs.00930. PMID 14657270.
  3. ^ a b Ebnet K (October 2017). "Junctional Adhesion Molecules (JAMs): Cell Adhesion Receptors With Pleiotropic Functions in Cell Physiology and Development". Physiological Reviews. 97 (4): 1529–1554. doi:10.1152/physrev.00004.2017. PMID 28931565. S2CID 10846721.
  4. ^ Lee HJ, Zheng JJ (May 2010). "PDZ domains and their binding partners: structure, specificity, and modification". Cell Communication and Signaling. 8 (1): 8. doi:10.1186/1478-811X-8-8. PMC 2891790. PMID 20509869.