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A more recent version of this article appeared on May 1, 2004
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Submitted on December 12, 2003
Revised on February 17, 2004
Accepted on February 23, 2004
q/11 Association
1 Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115
* Corresponding author. E-mail address: martin_hemler{at}dfci.harvard.edu.
By means of a variety of intracellular scaffolding proteins, a vast number of heterotrimeric G protein coupled receptors (GPCRs) may achieve specificity in signaling through a much smaller number of heterotrimeric G proteins. Members of the tetraspanin family organize extensive complexes of cell surface proteins and thus have the potential to act as GPCR scaffolds; however, tetraspanin-GPCR complexes had not previously been described. We now show that a GPCR, GPR56/TM7 x N1, and heterotrimeric G protein subunits, G
q, G11, and G
associate specifically with tetraspanins CD9 and CD81, but not with other tetraspanins. Complexes of GPR56 with CD9 and CD81 remained intact when fully solubilized and were resistant to cholesterol depletion. Hence they do not depend upon detergent-insoluble, raft-like membrane microdomains for stability. A central role for CD81 in promoting or stabilizing a GPR56-CD81-Gq/11 complex was revealed by CD81 immunodepletion and reexpression experiments. Finally, antibody engagement of cell surface CD81 or cell activation with phorbol ester revealed two distinct mechanisms by which GPR56-CD81-Gq/11 complexes can be dynamically regulated. These data reveal a potential role for tetraspanins CD9 and CD81 as GPCR scaffolding proteins.
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