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3
1 with CD151 Provides a Major Link to
Phosphatidylinositol 4-Kinase, and May Regulate Cell Migration
*Department of Cancer Immunology and AIDS, Dana-Farber Cancer
Institute and Department of Pathology, Harvard Medical School, Boston,
Massachusetts 02115;
Here we describe an association between The University of Birmingham,
CRC Institute for Cancer Studies, Birmingham, United Kingdom B15
2TA; and
§Department of Surgical Research, Rhode Island
Hospital, Providence, Rhode Island 02903
3
1 integrin
and transmembrane-4 superfamily (TM4SF) protein CD151. This association is maintained in relatively stringent detergents and thus is remarkably stable in comparison with previously reported integrin-TM4SF
protein associations. Also, the association is highly specific (i.e., observed in vitro in absence of any other cell surface proteins), and
highly stoichiometric (nearly 90% of 31 associated with CD151).
In addition, 31 and CD151 appeared in parallel on many cell lines
and showed nearly identical skin staining patterns. Compared with other
integrins, 31 exhibited a considerably higher level of
associated phosphatidylinositol-4-kinase (PtdIns 4-kinase) activity, most of which was removed upon immunodepletion of CD151. Specificity for CD151 and PtdIns 4-kinase association resided in the
extracellular domain of 31, thus establishing a
novel paradigm for the specific recruitment of an
intracellular signaling molecule. Finally, antibodies to
either CD151 or 31 caused a ~88-92% reduction in neutrophil
motility in response to f-Met-Leu-Phe on fibronectin, suggesting
an functionally important role of these complexes in cell migration.
These authors contributed equally to this work.
Corresponding author.
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