JCB logo
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 385K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Arregui, C.
Right arrow Articles by Balsamo, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Arregui, C.
Right arrow Articles by Balsamo, J.
Right arrowPubmed/NCBI databases
*OMIM
*Substance via MeSH
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/2000//1263 $5.00
The Journal of Cell Biology, Volume 149, Number 6, , 2000 1263-1274

Original Article

The Nonreceptor Tyrosine Kinase Fer Mediates Cross-Talk between N-Cadherin and β1-Integrins



Carlos Arreguia, Purnima Pathrea, Jack Liliena, and Janne Balsamoa

a Department of Biological Sciences, Wayne State University, Detroit, Michigan 48202
Department of Biological Sciences, Wayne State University, Detroit, MI 48202.(313) 577-6891(313) 577-0133

jlilien{at}biology.biosci.wayne.edu

Cadherins and integrins must function in a coordinated manner to effectively mediate the cellular interactions essential for development. We hypothesized that exchange of proteins associated with their cytoplasmic domains may play a role in coordinating function. To test this idea, we used Trojan peptides to introduce into cells and tissues peptide sequences designed to compete for the interaction of specific effectors with the cytoplasmic domain of N-cadherin, and assayed their effect on cadherin- and integrin-mediated adhesion and neurite outgrowth. We show that a peptide mimicking the juxtamembrane (JMP) region of the cytoplasmic domain of N-cadherin results in inhibition of N-cadherin and β1-integrin function. The effect of JMP on β1-integrin function depends on the expression of N-cadherin and is independent of transcription or translation. Treatment of cells with JMP results in the release of the nonreceptor tyrosine kinase Fer from the cadherin complex and its accumulation in the integrin complex. A peptide that mimics the first coiled-coil domain of Fer prevents Fer accumulation in the integrin complex and reverses the inhibitory effect of JMP. These findings suggest a new mechanism through which N-cadherin and β1-integrins are coordinately regulated: loss of an effector from the cytoplasmic domain of N-cadherin and gain of that effector by the β1-integrin complex.

Key Words: cadherin • integrin • Trojan peptides • adhesion • neurite outgrowth

© 2000 The Rockefeller University Press

The present address of Carlos Arregui is INTECH, Camino Circunvalación Km 6, CC164, 7130 Chascomús, Argentina. The present address of J. Lilien and J. Balsamo is Department of Biological Sciences, University of Iowa, Iowa City, IA 52242-1324.

Abbreviations used in this paper: CBP, catenin binding peptide; COP, control antennapedia peptide; FCC, Fer coiled-coil domain peptide; FNT, Fer NH2-terminal peptide; JMP, juxtamembrane peptide; LN, L cells expressing N-cadherin; SBP, Shc binding region peptide.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents