Title: Selective anchoring in the specific plasma membrane domain: a role in epithelial cell polarity Document date: 1988_12_1
ID: tyb0g7pz_31
Snippet: Recently, Nelson and Veshnock (48, 49) have shown that the development of an insoluble fodrin network on the basolateral membrane correlates with the polarization of the basolateral marker Na+-K + ATPase which forms a stable complex with ankyrin and fodrin (50) . We found that destabilization of this network by 4 mM DTT significantly facilitated extraction of B1, but not A1 (Table HI) . Thus, this result and the detergent extractability of B1 and.....
Document: Recently, Nelson and Veshnock (48, 49) have shown that the development of an insoluble fodrin network on the basolateral membrane correlates with the polarization of the basolateral marker Na+-K + ATPase which forms a stable complex with ankyrin and fodrin (50) . We found that destabilization of this network by 4 mM DTT significantly facilitated extraction of B1, but not A1 (Table HI) . Thus, this result and the detergent extractability of B1 and B2 in cells prevented from forming cell-cell contacts, are compatible with a basolateral fodrin cytoskeleton (4, 73) anchoring B1 but not A1.
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