Journal of Cell Science 116, e102-e102 (2003)
Copyright © 2003 The Company of Biologists Limited
Nectinafadin: a new adhesion system
Intercellular junctions are essential for maintenance of tissue integrity
and play key roles in morphogenesis, proliferation and cell migration. Indeed
desmosomes, tight junctions and cadherin-based adherens junctions are covered
in pretty much every basic cell biology textbook. Less well known is the
nectinafadin system. In a Commentary on
p. 17, Yoshimi Takai and
Hiroyuki Nakanishi review the roles of this novel type of intercellular
junction. Nectin is a Ca2+-independent, transmembrane adhesion
molecule that contains three extracellular immunoglobulin-like domains, which
can interact with other nectin molecules on the same cell or on a neighbouring
cell. Afadin is a cytoplasmic adaptor that connects nectin to the actin
cytoskeleton and might also interact with signalling molecules. The
nectinafadin system is associated with adherens junctions in
fibroblasts and epithelial cells, and studies of nectin mutants and knockout
work indicate that it is important for organization of both adherens junctions
and tight junctions. The system also appears to play a part in organization of
synapses and sertoli-cellspermatid junctions and is thus implicated in
both homotypic and heterotypic cell-cell adhesion.
Related articles in JCS:
- Nectin and afadin: novel organizers of intercellular junctions
- Yoshimi Takai and Hiroyuki Nakanishi
JCS 2003 116: 17-27.
[Abstract]
[Full Text]