Nectins and nectin‐like molecules: Roles in cell adhesion, polarization, movement, and proliferation
Open Access
- 1 May 2006
- journal article
- review article
- Published by Wiley in IUBMB Life
- Vol. 58 (5-6), 334-343
- https://doi.org/10.1080/15216540600719622
Abstract
Nectins and nectin‐like molecules (Necls) are immunoglobulin‐like cell adhesion molecules that constitute families containing four and five members, respectively. All members, except for Necl‐5, trans‐interact homophilically. Furthermore, all members, including Necl‐5, trans‐interact heterophilically with their respective specific partners among the members. Necl‐5 regulates cell movement and proliferation cooperatively with integrin αvβ3 and growth factor receptors. Nectins function as cell‐cell adhesion molecules at a variety of cell‐cell junctions, including adherens junctions, and regulate the initial step of cell‐cell junction formation. Nectins and integrin αvβ3 are further involved in the cross‐talk between cell‐matrix and cell‐cell junctions. Thus, both nectin and Necl family members play important roles in fundamental cellular functions, including cell adhesion, polarization, movement, and proliferation. iubmb Life, 58: 334‐343, 2006Keywords
This publication has 48 references indexed in Scilit:
- The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell responses through the cell-surface receptor CRTAMBlood, 2005
- Regulation of E-cadherin Endocytosis by Nectin through Afadin, Rap1, and p120ctnJournal of Biological Chemistry, 2005
- Vav2 as a Rac-GDP/GTP Exchange Factor Responsible for the Nectin-induced, c-Src- and Cdc42-mediated Activation of RacPublished by Elsevier ,2005
- Involvement of the c-Src-Crk-C3G-Rap1 Signaling in the Nectin-induced Activation of Cdc42 and Formation of Adherens JunctionsJournal of Biological Chemistry, 2005
- Rap1 Regulates E-cadherin-mediated Cell-Cell AdhesionJournal of Biological Chemistry, 2004
- Roles played by a subset of integrin signaling molecules in cadherin-based cell–cell adhesionThe Journal of cell biology, 2004
- Nectin-like Molecule-5/Tage4 Enhances Cell Migration in an Integrin-dependent, Nectin-3-independent MannerPublished by Elsevier ,2004
- Tage4/Nectin-like Molecule-5 Heterophilically trans-Interacts with Cell Adhesion Molecule Nectin-3 and Enhances Cell MigrationJournal of Biological Chemistry, 2003
- Nectin4/PRR4, a New Afadin-associated Member of the Nectin Family That Trans-interacts with Nectin1/PRR1 through V Domain InteractionJournal of Biological Chemistry, 2001
- Nectin-3, a New Member of Immunoglobulin-like Cell Adhesion Molecules That Shows Homophilic and Heterophilic Cell-Cell Adhesion ActivitiesJournal of Biological Chemistry, 2000