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Interaction with and regulation of the SLC26 transporters by CFTR. The structures of…
Figure 1.
Interaction with and regulation of the SLC26 transporters by CFTR. The structures of the unphosphorylated CFTR (5UAK) and the phosphorylated CFTR (6MSM) were taken from Zhang et al., and of Slc26a9 (6RTF) from Walter et al. In the inactive state, the R domain of CFTR prevents the interaction of the NBDs and is not available for interaction with other proteins. The basal activity of the SLC26 transporters, including pendrin, is low with the two STAS domains of the two monomers interacting with each other. An increase in cAMP and activation of PKA phosphorylates the R domain, resulting in the swinging of the R domain and its interaction with the STAS domain, which can facilitate and stabilize the interaction of the nucleotide binding clefts to activate CFTR. Interaction of the R domain with the STAS domain stabilizes expression and activates the SLC26 transporters. NBD, nucleotide binding domain; TMD, transmembrane domain.
Lee MG, Ohana E, Park HW, Yang D, Muallem S: Molecular mechanism of pancreatic and salivary gland fluid and HCO3 secretion. Physiol Rev 92: 39–74, 2012.
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