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Updated: Apr 18, 2026

The CryoAPEX Method for Electron Microscopy Analysis of Membrane Protein Localization Within Ultrastructurally-Preserved Cells
Published on: February 27, 2020
AKAP350C targets to mitochondria via a novel amphipathic alpha helical domain
Twila A Mason1, James R Goldenring2, Elena Kolobova3
1Departments of Cell and Developmental Biology; Vanderbilt University Medical Center ; Nashville, TN USA ; Epithelial Biology Center; Vanderbilt University Medical Center ; Nashville, TN USA.
Abstract:
Mitochondria regulate metabolism and homeostasis within cells. Mitochondria are also very dynamic organelles, constantly undergoing fission and fusion. The importance of maintaining proper mitochondrial dynamics is evident in the various diseases associated with defects in these processes. Protein kinase A (PKA) is a key regulator of mitochondrial dynamics. PKA is spatially regulated by A-Kinase Anchoring Proteins (AKAPs). We completed cloning of a novel AKAP350 isoform, AKAP350C. Immunostaining for endogenous AKAP350C showed localization to mitochondria. The carboxyl-terminal 54-amino acid sequence unique to AKAP350C contains a novel amphipathic alpha helical mitochondrial-targeting domain. AKAP350C co-localizes with Mff (mitochondrial fission protein) and mitofusins 1 and 2 (mitochondrial fusion proteins), and likely regulates mitochondrial dynamics by scaffolding PKA and mitochondrial fission and fusion proteins.
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