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Vol. 8, Issue 11, 2253-2265, November 1997
6A
1 Induces CD81-dependent Cell
Motility without Engaging the Extracellular Matrix Migration
Substrate
and
Departments of
*Cell Biology and
It is well established that integrins and extracellular
matrix (ECM) play key roles in cell migration, but the underlying mechanisms are poorly defined. We describe a novel mechanism whereby the integrin Immunology, The
Scripps Research Institute, La Jolla, California 92037
6
1, a laminin receptor, can affect cell
motility and induce migration onto ECM substrates with which it is not engaged. By using DNA-mediated gene transfer, we expressed the human
integrin subunit 6A in murine embryonic stem (ES) cells. ES
cells expressing 6A (ES6A) at the surface dimerized with endogenous 1, extended numerous filopodia and lamellipodia, and were intensely migratory in haptotactic assays on laminin (LN)-1. Transfected 6A
was responsible for these effects, because cells transfected with
control vector or 6B, a cytoplasmic domain 6 isoform, displayed compact morphology and no migration, like wild-type ES cells. The ES6A
migratory phenotype persisted on fibronectin (Fn) and Ln-5. Adhesion
inhibition assays indicated that 61 did not contribute detectably
to adhesion to these substrates in ES cells. However, anti-6
antibodies completely blocked migration of ES6A cells on Fn or Ln-5.
Control experiments with monensin and anti-ECM antibodies indicated
that this inhibition could not be explained by deposition of an
61 ligand (e.g., Ln-1) by ES cells. Cross-linking with secondary
antibody overcame the inhibitory effect of anti-6 antibodies,
restoring migration or filopodia extension on Fn and Ln-5. Thus, to
induce migration in ES cells, 6A1 did not have to engage with an
ECM ligand but likely participated in molecular interactions sensitive
to anti-61 antibody and mimicked by cross-linking. Antibodies to
the tetraspanin CD81 inhibited 6A1-induced migration but had no
effect on ES cell adhesion. It is known that CD81 is physically
associated with 61, therefore our results suggest a mechanism by
which interactions between 6A1 and CD81 may up-regulate cell
motility, affecting migration mediated by other integrins.
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