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Vol. 13, Issue 3, 767-781, March 2002
and
*Dana-Farber Cancer Institute and Department of Pathology, Harvard
Medical School, Boston, Massachusetts 02115; and
Here we demonstrate that multiple tetraspanin (transmembrane 4 superfamily) proteins are palmitoylated, in either the Golgi or a
post-Golgi compartment. Using CD151 as a model tetraspanin, we
identified and mutated intracellular N-terminal and C-terminal cysteine
palmitoylation sites. Simultaneous mutations of C11, C15, C242, and
C243 (each to serine) eliminated >90% of CD151 palmitoylation.
Notably, palmitoylation had minimal influence on the density of
tetraspanin protein complexes, did not promote tetraspanin localization
into detergent-resistant microdomains, and was not required for
CD151-Children's Hospital and Department of Pediatrics,
Harvard Medical School, Boston, Massachusetts 02115
3
1 integrin association. However, the CD151 tetra
mutant showed markedly diminished associations with other cell surface
proteins, including other transmembrane 4 superfamily proteins (CD9,
CD63). Thus, palmitoylation may be critical for assembly of the large
network of cell surface tetraspanin-protein interactions, sometimes
called the "tetraspanin web." Also, compared with wild-type CD151,
the tetra mutant was much more diffusely distributed and showed
markedly diminished stability during biosynthesis. Finally, expression
of the tetra-CD151 mutant profoundly altered 3
integrin-deficient kidney epithelial cells, such that they converted from a dispersed, elongated morphology to an epithelium-like cobblestone clustering. These results point to novel biochemical and
biological functions for tetraspanin palmitoylation.
Corresponding author. E-mail address:
MartinHemler{at}DFCI.Harvard.EDU.
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