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Published 11 October 2004. doi:10.1083/jcb.200312166
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 1, 161-170
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Article

 Spermidine/spermine N1-acetyltransferase specifically binds to the integrin {alpha}9 subunit cytoplasmic domain and enhances cell migration

Chun Chen1, Bradford A. Young1, Catherine S. Coleman2, Anthony E. Pegg2, and Dean Sheppard1

1 Lung Biology Center, Department of Medicine, University of California, San Francisco, San Francisco, CA 94110
2 Department of Cellular and Molecular Physiology, College of Medicine, The Pennsylvania State University, Hershey, PA 17033

Correspondence to Dean Sheppard: deans{at}itsa.ucsf.edu

The integrin {alpha}9ß1 is expressed on migrating cells, such as leukocytes, and binds to multiple ligands that are present at sites of tissue injury and inflammation. {alpha}9ß1, like the structurally related integrin {alpha}4ß1, mediates accelerated cell migration, an effect that depends on the {alpha}9 cytoplasmic domain. {alpha}4ß1 enhances migration through reversible binding to the adapter protein, paxillin, but {alpha}9ß1-dependent migration is paxillin independent. Using yeast two-hybrid screening, we identified the polyamine catabolizing enzyme spermidine/spermine N1-acetyltransferase (SSAT) as a specific binding partner of the {alpha}9 cytoplasmic domain. Overexpression of SSAT increased {alpha}9ß1-mediated migration, and small interfering RNA knockdown of SSAT inhibited this migration without affecting cell adhesion or migration that was mediated by other integrin cytoplasmic domains. The enzyme activity of SSAT is critical for this effect, because a catalytically inactive version did not enhance migration. We conclude that SSAT directly binds to the {alpha}9 cytoplasmic domain and mediates {alpha}9-dependent enhancement of cell migration, presumably by localized effects on acetylation of polyamines or of unidentified substrates.

Abbreviations used in this paper: BE-3-3-3, N1,N11-bis(ethyl)norspermine tetrahydrochloride; HMVEC, human microvascular endothelial cells; MEF, mouse embryonic fibroblast; PAO, polyamine oxidase; siRNA, small interfering RNA; SSAT, spermidine/spermine N1-acetyltransferase.


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