Mitochondria, as the central organelle responsible for cellular energy supply and metabolic regulation, play a crucial role in maintaining cellular homeostasis through their quality control mechanisms. Mitochondrial quality control abnormalities can lead to cellular damage and dysfunction, directly contributing to the development of aging-related diseases such as cancer and cardiovascular diseases. A kinase anchoring protein 1 (AKAP1), as an anchoring protein localized to the outer mitochondrial membrane, also participates in regulating important biological processes such as mitochondrial structure and function, mitochondrial dynamics, and mitophagy. Recent studies show that AKAP1 interacts with ubiquinone oxidoreductase core subunit S1 (NDUFS1) and manganese superoxide dismutase (MnSOD) to maintain mitochondrial cristae structure, membrane potential, and respiratory function, and exerts antioxidant stress resistance. Furthermore, AKAP1 not only promotes mitochondrial fusion, but also interacts with estrogen receptor β (ERβ), protein kinase A (PKA), calcineurin (CaN), tribbles pseudo kinase 3 (TRIB3), and dynamin-related protein 1 (Drp1) to promote or inhibit mitochondrial fission. In addition, AKAP1 binds to PKA and activates the protein kinase B (AKT)/ endothelial nitric oxide synthase (eNOS) signaling pathway to inhibit excessive mitophagy. This article reviews the role and mechanism of AKAP1 in regulating mitochondrial quality control, aiming to provide valuable insights for the development and application of AKAP1-targeted drugs and exercise interventions. Firstly, as an outer mitochondrial membrane protein, AKAP1 is involved in maintaining the stability of mitochondrial crista structure, and its gene deletion will cause the loss and breakage of crista. Secondly, AKAP1 is also involved in maintaining mitochondrial membrane potential and oxidative phosphorylation function. mRNAs of short proteins, especially eukaryotic-origin electron transport chain (ETC) components, are specifically recruited by AKAP1 in a translation-independent manner that depends on mRNA splicing. AKAP1 loss can lower ETC levels, but its gene overexpression can reduce the production of reactive oxygen species (ROS) and enhance the mitochondrial membrane potential, the activity of respiratory chain complex I, and respiratory function. Thirdly, AKAP1 participates in the positive regulation of mitochondrial fusion, but its role in mitochondrial fission may be dependent on specific cell types, as it can promote or inhibit the mitochondrial fission by increasing phosphorylation of Drp1^Ser637. The effect and mechanism of AKAP1 on regulating other phosphorylation sites of Drp1 (e.g. Drp1^Ser616) and mitochondrial fusion proteins (e.g. mitofusion1/2 (Mfn1/2), OPA1) are unclear. Further studies on mitochondrial fusion/fission imbalance-related diseases (such as cardiovascular diseases and breast cancer) can be carried out to clarify the mechanism of AKAP1 in the pathological process and the relationship between AKAP1 and mitochondrial dynamic proteins in different tissues. Finally, AKAP1 can activate the AKT/eNOS signaling pathway and interact with PKA under the conditions of PTEN-induced putative kinase protein 1 (PINK1) gene deletion, thereby inhibiting excessive mitophagy. Future research can explore whether there are more mitophagy-related proteins (such as NIX, BNIP3, FUNDC1, etc.) involved and their association with AKAP1 by constructing tissue-specific PINK1 single knockout and PINK1/AKAP1 double knockout models. In addition, the molecular mechanism by which AKAP1 mediates the translocation of NDUFS1, PKA, and Drp1 from cytoplasm to mitochondria is unclear. In future research, it is necessary to elucidate how AKAP1 specifically recognizes its interacting proteins based on the cellular environment.