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J. Biol. Chem., Vol. 269, Issue 28, 18311-18314, 07, 1994
ME Lukashev, D Sheppard and R Pytela
The cytoplasmic domains of integrin beta subunits are essential for the
function of integrins in cell adhesion and signaling. A chimera combining
the transmembrane and cytoplasmic domains of the beta 1 integrin subunit
with an irrelevant extracellular domain derived from L3T4 (murine CD4) was
tested for its ability to interfere with integrin function. Expression of
this construct in cultured human embryonic kidney cells under the control
of the inducible metallothionein promoter resulted in cell rounding and
detachment, and blocked cell adhesion mediated by the beta 1 and alpha v
beta 5 integrins. Expression of the beta 1 chimera at basal levels
interfered with the tyrosine phosphorylation of a 125-kDa protein induced
by antibody- induced clustering of integrins. Induced expression of the
chimera resulted in sustained tyrosine phosphorylation of this protein,
which could be enhanced by clustering of the chimera but was insensitive to
clustering of integrins. These results demonstrate that the autonomously
expressed beta 1 integrin cytoplasmic domain can act as a trans-dominant
inhibitor of integrin function, presumably via competitive interactions
with cytoplasmic components that are required for integrin-mediated cell
adhesion and tyrosine phosphorylation.
Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed beta 1 integrin cytoplasmic domain
Department of Medicine, University of California, San Francisco 94143.
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