PRKACB
Description
The PRKACB (protein kinase cAMP-activated catalytic subunit beta) is a protein-coding gene located on chromosome 1.
PRKACB gene encodes cAMP-dependent protein kinase catalytic subunit beta, an enzyme crucial for various cellular functions. cAMP activates PKA, a tetrameric protein composed of regulatory and catalytic subunits. cAMP binding triggers dissociation of the inactive holoenzyme into active catalytic subunits. PRKACB belongs to the serine/threonine protein kinase family and exists in three isoforms due to alternative splicing. PRKACB interacts with Ryanodine receptor 2 and Low affinity nerve growth factor receptor.
PRKACB, also known as PKA C-beta, mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates various cellular processes like cell proliferation, cell cycle, differentiation, microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, intracellular transport, and ion flux. PRKACB regulates the abundance of its regulatory subunits by phosphorylating PJA2, leading to ubiquitination and proteolysis of these subunits. It also phosphorylates GPKOW, modulating its RNA binding ability. Moreover, PRKACB acts as a negative regulator of mTORC1 through phosphorylation of RPTOR.
PRKACB is also known as CAFD2, PKA C-beta, PKACB.
