RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1.

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Citation

Denti S, Sirri A, Cheli A, Rogge L, Innamorati G, Putignano S, Fabbri M, Pardi R, Bianchi E

RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1.

J Biol Chem. 2004 Mar 26;279(13):13027-34. Epub 2004 Jan 13.

PubMed ID
14722085 [ View in PubMed
]
Abstract

Integrin adhesion receptors can act as signaling receptors that transmit information from the extracellular environment to the interior of the cell, affecting many fundamental cellular processes, such as cell motility, proliferation, differentiation, and survival. Integrin signaling depends on the formation of organized sub-membrane complexes that comprise cytoskeletal, adapter, and signaling molecules. The identification of molecules that interact with the cytoplasmic domain of integrins has been the focus of research aimed to elucidating the mechanistic basis of integrin signal transduction. We have identified RanBPM as a novel interactor of the beta(2) integrin LFA-1 in a yeast-two-hybrid screen. In the same assay, RanBPM also interacted with the beta(1) integrin cytoplasmic domain. We demonstrate that RanBPM is a peripheral membrane protein and that integrins and RanBPM interact in vitro and in vivo and co-localize at the cell membrane. We find that RanBPM is phosphorylated on serine residues; phosphorylation of RanBPM is increased by stress stimuli and decreased by treatment with the p38 kinase inhibitor SB203580. Transfection of RanBPM synergizes with LFA-1-mediated adhesion in the transcriptional activation of an AP-1-dependent promoter, indicating that the two proteins interact functionally as well. We suggest that RanBPM may constitute a molecular scaffold that contributes to coupling LFA-1 and other integrins with intracellular signaling pathways.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Integrin beta-2P05107Details
Integrin beta-1P05556Details