Mechanisms underlying regulated CFTR trafficking.
Stimulation of membrane capacitance and cell surface labeling of epitope-tagged CFTR provide evidence of cAMP-regulated CFTR trafficking. Co-expression of syntaxin 1A inhibits cAMP-stimulated current and capacitance changes in CFTR expressing cells and blocks cAMP-induced increases in cell surface CFTR. Inhibition of CFTR trafficking by syntaxin over-expression suggests a role for SNARE proteins in this process. CFTR phosphorylation may alter physical interactions with SNARE proteins to regulate plasma membrane CFTR density.
Peters
K W
KW
Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, Pennsylvania, USA.
Qi
J
J
Watkins
S C
SC
Frizzell
R A
RA
D000242:Cyclic AMP / Q000502:physiology; D003550:Cystic Fibrosis / Q000235:genetics*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000235:genetics*; D005786:Gene Expression Regulation / Q000502:physiology; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics; D050765:Qa-SNARE Proteins; D050827:Syntaxin 1
C505032:CFTR protein, human; D008565:Membrane Proteins; D050765:Qa-SNARE Proteins; C494212:STX1A protein, human; D050827:Syntaxin 1; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D000242:Cyclic AMP