Title

Formation Of A Β1 Integrin Signaling Complex In Schwann Cells Is Independent Of Rho

Keywords

Differentiation; Focal adhesion; Myelination

Abstract

Schwann cell adhesion to basal lamina is essential for peripheral nerve development. β1 integrin receptors for extracellular matrix cooperate with other receptors to transmit signals that coordinate cell cycle progression and initiation of differentiation, including myelin-specific gene expression. In Schwann cell/sensory neuron cocultures, β1 integrins complex with focal adhesion kinase (FAK), fyn kinase, paxillin, and schwannomin in response to basal lamina adhesion. To study the assembly of this signaling complex in Schwann cells (SCs), we induced β1 integrin clustering on suspended cells using an immobilized antibody and recovered a complex containing β1 integrin, FAK, paxillin, and schwannomin. In adherent subconfluent cells, the proteins colocalized to filopodia, ruffling membranes and focal contacts. We assessed the role of rhoGTPase in the process of integrin complex assembly by introducing C3 transferase (C3T), a rho inhibitor, into the cells. Although C3T caused dose-dependent morphological abnormalities, FAK, paxillin, and schwannomin were able to coimmunoprecipitate with β1 integrin. Additionally, colocalization of FAK, paxillin, and schwannomin with β1 integrin in filopodia and small focal contacts remained unchanged. We conclude that SCs do not require active rho to recruit signaling and structural proteins to β1 integrins clustered at the plasma membrane. Rho is required to establish large focal adhesions and to spread and stabilize plasma membrane extensions. © 2003 Wiley-Liss, Inc.

Publication Date

1-1-2003

Publication Title

GLIA

Volume

41

Issue

1

Number of Pages

94-104

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1002/glia.10170

Socpus ID

0037207511 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/0037207511

This document is currently not available here.

Share

COinS