The immunoglobulin-like cell adhesion molecule nectin and its associated protein afadin.

@article{Takai2008TheIC,
  title={The immunoglobulin-like cell adhesion molecule nectin and its associated protein afadin.},
  author={Yoshimi Takai and Wataru Ikeda and Hisakazu Ogita and Yoshiyuki Rikitake},
  journal={Annual review of cell and developmental biology},
  year={2008},
  volume={24},
  pages={
          309-42
        }
}
  • Y. Takai, W. Ikeda, +1 author Y. Rikitake
  • Published 6 October 2008
  • Biology, Chemistry, Medicine
  • Annual review of cell and developmental biology
Nectins are immunoglobulin-like cell adhesion molecules (CAMs) that compose a family of four members. Nectins homophilically and heterophilically interact in trans with each other to form cell-cell adhesions. In addition, they heterophilically interact in trans with other immunoglobulin-like CAMs. Nectins bind afadin, an actin filament (F-actin)-binding protein, at its cytoplasmic tail and associate with the actin cytoskeleton. Afadin additionally serves as an adaptor protein by further binding… 
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Nectins have recently been identified as new cell adhesion molecules (CAMs) consisting of four members. They show immunoglobulin-like structures and exclusively localize at adherens junctions (AJs)…
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TLDR
Of the three types of nectin-mediated cell adhesions, the afadin- and cadherin-dependent apparatus has been most extensively investigated, but the examples of the third type of apparatus independent of afadin and caderin are recently increasing and its morphological and functional properties have been well characterized.
Immunoglobulin superfamily receptors and adherens junctions.
TLDR
The immunogroblin (Ig) superfamily proteins characterized by the presence of Ig-like domains are involved in various cellular functions and play important roles in the regulation of many cellular functions, such as cell polarization, movement, proliferation, differentiation, survival, and cell sorting.
Nectin family of cell-adhesion molecules: structural and molecular aspects of function and specificity
TLDR
Current structural and molecular knowledge of nECTin recognition processes are reviewed, with a focus on the biochemical and biophysical determinants of affinity and selectivity that drive distinct nectin associations.
Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules
TLDR
The structure of a Necl heterodimer comprising the ectodomains of mouse Necl4 and Necl1 is determined, providing groundbreaking structural insights into Necl heterogeneity and a model of Necl binding specificity that involves an induced-fit conformational change at the dimerization interface is proposed.
Binding between the Junctional Proteins Afadin and PLEKHA7 and Implication in the Formation of Adherens Junction in Epithelial Cells*
TLDR
This study showed that PLEKHA7 bound to afadin in addition to p120ctn and was recruited to the nectin-3α-based cell-cell adhesion site in a manner dependent on afadin, but not on p 120ctn.
Membrane palmitoylated proteins regulate trafficking and processing of nectins.
Roles of nectins and nectin-like molecules in the nervous system.
TLDR
Nectins are immunoglobulin-like cell adhesion molecules (CAMs) constituting a family with four members that are involved in the formation of various kinds of cell-cell adhesion and diverse cellular functions including cell polarization, movement, proliferation, survival, and differentiation.
Afadin/AF-6 and canoe: roles in cell adhesion and beyond.
Nectin-1 Binds and Signals through the Fibroblast Growth Factor Receptor*
TLDR
The structure in solution of the third, membrane-proximal Ig module of mouse nectin-1 (nectin- 1 Ig3) solved by means of nuclear magnetic resonance (NMR) spectroscopy is reported and it is suggested that FGFR is a downstream signaling partner of nectIn-1.
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References

SHOWING 1-10 OF 224 REFERENCES
Interaction of Integrin αvβ3 with Nectin
TLDR
It is shown that integrin αvβ3 functionally and physically associates with nectin and play pivotal roles in the cross-talk between cell-matrix and cell-cell junctions and the formation of cadherin-based AJs.
Two Cell Adhesion Molecules, Nectin and Cadherin, Interact through Their Cytoplasmic Domain–Associated Proteins
TLDR
It is shown here that nectin and E-cadherin were colocalized through l-afadin and the COOH-terminal half of α-catenin at AJs and suggest that these two cell–cell adhesion systems cooperatively organize cell– cell AJs.
Involvement of LMO7 in the Association of Two Cell-Cell Adhesion Molecules, Nectin and E-cadherin, through Afadin and α-Actinin in Epithelial Cells*
TLDR
A rat counterpart of the human LIM domain only 7 (LMO7) is identified as an afadin- and α-actinin-binding protein that connects the nectin-afadin and E-cadherin-catenin systems through α- actinin.
Nectin-3, a New Member of Immunoglobulin-like Cell Adhesion Molecules That Shows Homophilic and Heterophilic Cell-Cell Adhesion Activities*
TLDR
The results indicate that the nECTin family consists of at least three members, nectin-1, -2, and -3, all of which show homophilic and heterophilic cell-cell adhesion activities and are localized at cadherin-based AJs.
Regulation of the Assembly and Adhesion Activity of E-cadherin by Nectin and Afadin for the Formation of Adherens Junctions in Madin-Darby Canine Kidney Cells*
TLDR
Nectin regulates the assembly and cell-cell adhesion activity of E-cadherin through afadin, nectin signaling, and p120ctn for the formation of AJs in Madin-Darby canine kidney cells.
Nectins and nectin‐like molecules: Roles in cell adhesion, migration, and polarization
TLDR
The roles and modes of action of nectin‐like molecules and necls in cell adhesion, migration, and polarization are reviewed.
Role of each immunoglobulin-like loop of nectin for its cell-cell adhesion activity.
Requirement of the actin cytoskeleton for the association of nectins with other cell adhesion molecules at adherens and tight junctions in MDCK cells
TLDR
Results indicate that the actin cytoskeleton is required for the association of the nectin‐afadin unit with other CAMs and PMPs at AJs and TJs.
Involvement of nectin in the localization of junctional adhesion molecule at tight junctions
TLDR
During the formation of the junctional complex consisting of AJs and TJs in Madin-Darby canine kidney cells, JAM was recruited to the nectin-based cell–cell adhesion sites andalyses of the localization and immunoprecipitation of JAM revealed that it was associated with nECTin through afadin and ZO-1.
Regulation of E-cadherin Endocytosis by Nectin through Afadin, Rap1, and p120ctn*[boxs]
TLDR
Results indicate that trans- interacting nectin inhibits non-trans-interacting E-cadherin endocytosis through afadin, Rap1, and p120ctn and thereby further accumulates non- trans-interacted E- cadher in to the nectIn-based cell-cell adhesion sites for the formation of AJs.
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