The cAMP-dependent Protein Kinase (PKA) is compartmentalized within the cell. To maintain the localization of PKA, the regulatory
subunits interact with specific anchoring proteins. Several proteins have been identified as PKA anchoring proteins and form a family named
AKAP (A-Kinase Anchor Proteins). Fifteen of the AKAP proteins contain a consensus binding motif that allows interaction with the type II
regulatory subunit (RII) of the PKA holoenzyme. In addition, three other AKAPs (D-AKAP1, D-AKAP2, and fsc1/AKAP82) can associate
with the type I regulatory subunit (RI) of the PKA holoenzyme. AKAP82 was isolated as a component of the mouse sperm fibrous sheath. It is
a dual specificity AKAP that contains an RII-binding domain (domain A; amino acids 219 to 232) and an RI-binding domain (domain B;
amino acids 335-344). In mouse, pro-AKAP82 is synthesized as a 97 kDa precursor that is transported to the flagellum where proteolytic
cleavage of the N-terminal 179 amino acids produces AKAP82. Assembly of AKAP82 into the fibrous sheath surrounding the axoneme of the
sperm flagellum is thought to tether PKA close to the axoneme where it can regulate flagellar motility.
原厂资料:
注意事项:
1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.