Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity

Elisabetta Bianchi (), Simona Denti, Alessandra Granata, Giovanna Bossi, Jens Geginat, Antonello Villa, Lars Rogge and Ruggero Pardi
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Elisabetta Bianchi: Scientific Institute San Raffaele-DIBIT
Simona Denti: Scientific Institute San Raffaele-DIBIT
Alessandra Granata: Scientific Institute San Raffaele-DIBIT
Giovanna Bossi: Sir William Dunn School of Pathology, University of Oxford
Jens Geginat: Scientific Institute San Raffaele-DIBIT
Antonello Villa: Scientific Institute San Raffaele-DIBIT
Lars Rogge: Roche Milano Ricerche
Ruggero Pardi: Scientific Institute San Raffaele-DIBIT

Nature, 2000, vol. 404, issue 6778, 617-621

Abstract: Abstract Integrin adhesion receptors transduce signals that control complex cell functions which require the regulation of gene expression, such as proliferation, differentiation and survival1. Their intracellular domain has no catalytic function, indicating that interaction with other transducing molecules is crucial for integrin-mediated signalling. Here we have identified a protein that interacts with the cytoplasmic domain of the β2 subunit of the αL/β2 integrin LFA-1. This protein is JAB1 (Jun activation domain-binding protein 1), a coactivator of the c-Jun transcription factor2. We found that JAB1 is present both in the nucleus and in the cytoplasm of cells and that a fraction of JAB1 colocalizes with LFA-1 at the cell membrane. LFA-1 engagement is followed by an increase of the nuclear pool of JAB1, paralleled by enhanced binding of c-Jun-containing AP-1 complexes to their DNA consensus site and increased transactivation of an AP-1-dependent promoter. We suggest that signalling through the LFA-1 integrin may affect c-Jun-driven transcription by regulating JAB1 nuclear localization. This represents a new pathway for integrin-dependent modulation of gene expression.

Date: 2000
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DOI: 10.1038/35007098

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