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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 385, Issue 10


Roles of nectins in cell adhesion, migration and polarization

Hiroyuki Nakanishi
  • Department of Molecular Pharmacology, Kumamoto University Graduate School of Medical Sciences, Kumamoto 860-8556, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Yoshimi Takai
  • Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Japan
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2004.116


Nectins are Ca2+-independent immunoglobulin (Ig)-like cell-cell adhesion molecules, which comprise a family consisting of four members. Nectins have five activities: (1) they show Ca2+-independent cell-cell adhesion activity by homo- and hetero-trans-interactions through their extracellular regions; (2) they bind afadin, an actin filament (F-actin)-binding protein, through their cytoplasmic tails and are connected to the actin cytoskeleton; (3) they induce activation of Cdc42 and Rac small G proteins through their cytoplasmic tails; (4) they bind Par-3, a cell polarity protein, through their cytoplasmic tails; and (5) they heterophilically trans-interact with Necls, nectin-like molecules, through their extracellular regions. Through these activities, nectins regulate a variety of cellular functions, including adhesion, migration, and polarization. Here we describe these activities and functions of nectins.

Keywords: cadherins; cell adhesion; cell migration; cell polarization; nectins; Necls

About the article

Published Online: 2005-06-01

Published in Print: 2004-10-01

Citation Information: Biological Chemistry, Volume 385, Issue 10, Pages 885–892, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2004.116.

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