[1] CPEB is present at postsynaptic sites and dendrites where it stimulates polyadenylation and translation in response to synaptic activity.

[2] CPEB most commonly activates the target RNA for translation, but can also act as a repressor,[3] dependent on its phosphorylation state.

[5] In animals, CPEB is expressed in several alternative splicing isoforms that are specific to particular tissues and functions, including the self-cleaving Mammalian CPEB3 ribozyme.

[9] In the nuclei of different organisms, it was found that CPEB helps guide the path of mRNA in the cytoplasm.

[9] CPEB can bind with CPE-containing mRNAs in the nucleus, which forces tight translational regulation in the cytoplasm.

The prion-like isoform of CPEB found in Aplysia californica, Drosophila, mice, and humans is an example of such differentiation.

[5] A misstep in the process of translation with CPEB can lead to possible adverse affects on neurological development.

Risk genes for autism spectrum disorder were found in brains where "...CPEB4 transcript isoform imbalance due to decreased inclusion of a neuronal-specific microexon together with a new molecular signature of global polyadenine tail shortening..."[14] In idiopathic autism spectrum disorder individuals, CPEB4 is greatly decreased and showed significant splicing alterations.

An equivalent isoform imbalance in mice mimics changes of autism spectrum disorder genes, which causes similar neuroanatomical, electrophysiological, and behavioral phenotype expression.

[15] When modeling fragile X syndrome in mice, CPEB1 gene mutations reduced pathological processes associated with the disorder.

However, CPEB sequestration translation dysfunction is not a definite cause of Huntington's disease symptoms in humans.

CPEB has been found to help regulate cellular senescence through modulating p53 mRNA polyadenylation-induced translation.

[17] When human skin and lung cells were put under a knockdown of CPEB, they bypassed the M1 crisis stage of senescence.

[18] These observations have led to the suggestion that long-lasting bistable prionlike proteins play a role in the formation of long-term memory.