期刊
MITOCHONDRION
卷 12, 期 4, 页码 423-427出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.mito.2012.04.004
关键词
Glycosylation; PDH E1 alpha; ANT; NDUFS3; ATP synthase subunit d; OSCP
资金
- NIH from the INBRE [P20 RR-016464, GM103440]
- NIH from the COBRE [P20 RR024210, GM103554]
- NIH [S10RR023587]
Nucleocytosolic and secreted proteins are commonly glycosylated. However, reports of glycosylated mitochondrial proteins are rare. Using lectin chromatography on bovine heart, we detected low-abundance glycoforms of nuclear-encoded proteins with well-established mitochondrial function: pyruvate dehydrogenase E1 alpha, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, ADP/ATP translocase, ATP synthase d and oligomycin sensitivity-conferring protein. Notably, the latter two have been previously detected at the plasma membrane. Our findings indicate that glycosylation of classic mitochondrial proteins may be more common than previously appreciated. We discuss the implication that glycosylation could represent an unexplored mechanism for regulating these proteins' functions within mitochondria or at extra-mitochondrial locations. (C) 2012 Elsevier B.V. and Mitochondria Research Society. All rights reserved.
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