Transhomodimerization of Nectins

Stable Identifier
Reaction [binding]
Homo sapiens
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Nectins are Ca(2+)-independent cell adhesion molecules which interact homophilically and heterophilically in trans to form cell-cell adhesions (reviewed in (Sakisaka et al., 2007; Takai et al., 2008). Each nectin first forms homo-cis-dimers and then homo- or hetero-trans-dimers through the extracellular region, causing cell–cell adhesion. The Nectin protein family is made up of four members, nectin-1, -2, -3, and -4, all of which have an extracellular region with three Ig-like loops, a single transmembrane region, and a cytoplasmic tail region.

Literature References
PubMed ID Title Journal Year
9845526 The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule

Lopez, M, Aoubala, M, Jordier, F, Isnardon, D, Gomez, S, Dubreuil, P

Blood 1998
10225955 Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein

Takahashi, K, Nakanishi, H, Miyahara, M, Mandai, K, Satoh, K, Satoh, A, Nishioka, H, Aoki, J, Nomoto, A, Mizoguchi, A, Takai, Y

J Cell Biol 1999
Participant Of
Orthologous Events