Journal
JOURNAL OF BIOCHEMISTRY
Volume 167, Issue 3, Pages 225-231Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvz090
Keywords
BioID; mass spectrometry; mitochondria; proteome; XL-MS
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan (JSPS KAKENHI) [17H03667, 17K19561, 18H04863, 17K08635, 18KK0229, 19H04966]
- Joint Usage and Joint Research Programs, the Institute of Advanced Medical Sciences, Tokushima University
- Grants-in-Aid for Scientific Research [19H04966, 18H04863, 17K08635, 17H03667, 17K19561, 18KK0229] Funding Source: KAKEN
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Protein-protein interactions are essential biologic processes that occur at inter- and intracellular levels. To gain insight into the various complex cellular functions of these interactions, it is necessary to assess them under physiologic conditions. Recent advances in various proteomic technologies allow to investigate protein-protein interaction networks in living cells. The combination of proximity-dependent labelling and chemical cross-linking will greatly enhance our understanding of multi-protein complexes that are difficult to prepare, such as organelle-bound membrane proteins. In this review, we describe our current understanding of mass spectrometry-based proteomics mapping methods for elucidating organelle-bound membrane protein complexes in living cells, with a focus on protein-protein interactions in mitochondrial subcellular compartments.
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