Bicarbonate-responsive "soluble" adenylyl cyclase defines a nuclear cAMP microdomain

J Cell Biol. 2004 Feb 16;164(4):527-34. doi: 10.1083/jcb.200311119. Epub 2004 Feb 9.

Abstract

Bicarbonate-responsive "soluble" adenylyl cyclase resides, in part, inside the mammalian cell nucleus where it stimulates the activity of nuclear protein kinase A to phosphorylate the cAMP response element binding protein (CREB). The existence of this complete and functional, nuclear-localized cAMP pathway establishes that cAMP signals in intracellular microdomains and identifies an alternate pathway leading to CREB activation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenylyl Cyclase Inhibitors
  • Adenylyl Cyclases / metabolism*
  • Animals
  • Bicarbonates / metabolism*
  • Cell Line
  • Cell Nucleus / enzymology*
  • Chlorocebus aethiops
  • Cyclic AMP / metabolism*
  • Cyclic AMP Response Element-Binding Protein / metabolism
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Enzyme Activation
  • Gene Expression Regulation
  • Hepatocytes / cytology
  • Hepatocytes / metabolism
  • Humans
  • Immunohistochemistry
  • Phosphorylation
  • Rats
  • Second Messenger Systems / physiology

Substances

  • Adenylyl Cyclase Inhibitors
  • Bicarbonates
  • Cyclic AMP Response Element-Binding Protein
  • Cyclic AMP
  • Cyclic AMP-Dependent Protein Kinases
  • Adenylyl Cyclases