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J Biol Chem, Vol. 273, Issue 27, 17221-17226, July 3, 1998
From the Institute of Biochemistry, University of Vienna, Vienna
Biocenter, A-1030 Vienna, Austria
The 31-kDa integral membrane protein stomatin
(protein 7.2b) is not only an important component of the red cell
membrane but can also be found in abundance in different tissues and
cell lines. The protein is thought to be anchored to the membrane by a
hydrophobic domain while both N and C termini are exposed to the
cytoplasm. We have previously shown in the human cell line UAC that
stomatin concentrates preferentially in plasma membrane folds and
protrusions. There is also evidence that stomatin is linked to the
cortical actin cytoskeleton, suggesting a role in cortical
morphogenesis of the cell. In this study, we demonstrate that the
fundamental structure of stomatin is oligomeric. Whereas interaction of
stomatin with itself was suggested by cross-linking experiments, we
show by density gradient centrifugation analysis that soluble
homo-oligomeric complexes of this protein are present in Triton X-100
extracts of UAC cells. We also show the existence of these oligomers by co-immunoprecipitation of the endogenous stomatin and a recombinantly expressed myc-tagged stomatin, using an anti-myc antibody. The data
indicate that these complexes comprise between 9 and 12 monomers of
stomatin. Two C-terminally truncated forms of stomatin do not incorporate into these oligomers, suggesting an involvement of the C
terminus in the homo-oligomeric interaction.
Oligomeric Nature of the Integral Membrane Protein Stomatin
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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