Models of secondary and quaternary structures of
CCE channels and their subunits. CCE channels are hypothesized to be
made of different Trps and/or different Trp combinations to account
for CCE channels with varying ion selectivities and different forms of
activation—e.g., store depletion-sensitive vs. store
depletion-insensitive. The transmembrane topology chosen is arbitrarily
based on that of voltage-gated K+, Na+, and
Ca2+ channels and is thus far supported by the finding that
hTrp3 is glycosylated and the results on HA localization in expression
experiments. However, other transmembrane topologies are possible and
the model may need major revisions. Existence of six nonallelic genes
encoding six Trp-related proteins, opens the possibility that there are
either diverse homomultimeric or diverse heteromultimeric CCE channels
that could account for the functional heterogeneity of CCE seen in
different tissues and cells.