Abstract:
:The observations described herein allow us to make several inferences about PKC and regulation of normal and CF Cl- channels. FIGURE 5 shows a model that summarizes these observations. In this model, for the sake of clarity, we refer to the channel as a single entity, but note that it may consist of multiple subunits and associated proteins. FIGURE 5A shows the channel in an inactivated state following excision from the cell. The channel can be activated by strong membrane depolarization, via an unknown mechanism, or by phosphorylation with PKA or PKC at a low [Ca2+] We speculate that PKA and PKC may phosphorylate and activate the channel at the same site, or region of the channel, because phosphorylation-dependent activation by both is defective in CF. This result suggests that the CF defect might lie in a defective phosphorylation site on the channel, or associated protein, or in the mechanism that converts phosphorylation into a change in channel conformation, such as activation. Activated channels can be inactivated by PKC at a high [Ca2+]. At high [Ca2+], PKC maintains the channel in an inactivated state and it inactivates channels that have been activated by PKC at low [Ca2+], by depolarization, or by PKA. Both activation and inactivation appear to result from phosphorylation; neither can be explained by down-regulation of the channel. There are several possible ways to explain the two opposite effects of PKC on the Cl- channel: different responses may be due to an effect of Ca2+ on the channel, on PKC, or on the interaction between the two.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Ann N Y Acad Scijournal_title
Annals of the New York Academy of Sciencesauthors
Welsh MJ,Li M,McCann JD,Clancy JP,Anderson MPdoi
10.1111/j.1749-6632.1989.tb25131.xsubject
Has Abstractpub_date
1989-01-01 00:00:00pages
44-51eissn
0077-8923issn
1749-6632journal_volume
574pub_type
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