cAMP induces dissociation of inactive PKA tetramers

Stable Identifier
R-HSA-111925
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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The protein kinase A (PKA) regulatory subunit isoforms differ in their tissue specificity and functional characteristics. The specific isoform activated in response to glucagon signaling is not known. The PKA kinase is a tetramer of two regulatory and two catalytic subunits. The regulatory subunits block the catalytic subunits. Binding of cAMP to the regulatory subunit triggers dissociation of the tetramer into two active dimers made up of a regulatory and a catalytic subunit.
Literature References
PubMed ID Title Journal Year
16407073 Dynamic binding of PKA regulatory subunit RI alpha

Kim, C, Taylor, SS, McCammon, JA, Gullingsrud, J

Structure 2006
Participants
Participates
Catalyst Activity

cAMP binding activity of PKA tetramer:4xcAMP [cytosol]

Orthologous Events
Authored
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Created
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