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D‐ AKAP 1a is a signal‐anchored protein in the mitochondrial outer membrane
Author(s) -
Jun YongWoo,
Park Heeju,
Lee YouKyung,
Kaang BongKiun,
Lee JinA,
Jang DeokJin
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12123
Subject(s) - microbiology and biotechnology , chemistry , mitochondrion , bacterial outer membrane , signal (programming language) , translocase of the inner membrane , biophysics , inner mitochondrial membrane , biochemistry , biology , mitochondrial membrane transport protein , computer science , escherichia coli , gene , programming language
Dual A‐kinase anchoring protein 1a (D‐ AKAP 1a, AKAP 1) regulates cAMP signaling in mitochondria. However, it is not clear how D‐ AKAP 1a is associated with mitochondria. In this study, we show that D‐ AKAP 1a is a transmembrane protein in the mitochondrial outer membrane ( MOM ). We revealed that the N‐terminus of D‐ AKAP 1a is exposed to the intermembrane space of mitochondria and that its C‐terminus is located on the cytoplasmic side of the MOM . Moderate hydrophobicity and the positively charged flanking residues of the transmembrane domain of D‐ AKAP 1a were important for targeting. Taken together, D‐ AKAP 1a can be classified as a signal‐anchored protein in the MOM . Our topological study provides valuable information about the molecular and cellular mechanisms of mitochondrial targeting of AKAP 1.

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