ArticleBiophysical journal2009
Mitochondrial creatine kinase binding to phospholipid monolayers induces cardiolipin segregation.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 31 citations in OpenAlex.
- Proteolipid domains form in biomimetic and cardiac mitochondrial vesicles and are regulated by cardiolipin concentration but not monolyso-cardiolipin.The Journal of biological chemistry · 2018Article
- Mechanisms by Which Dietary Fatty Acids Regulate Mitochondrial Structure-Function in Health and Disease.Advances in nutrition (Bethesda, Md.) · 2018Review
- Docosahexaenoic acid lowers cardiac mitochondrial enzyme activity by replacing linoleic acid in the phospholipidome.The Journal of biological chemistry · 2018Article
- The potent effect of mycolactone on lipid membranes.PLoS pathogens · 2018Article
- Cardiolipin in Central Nervous System Physiology and Pathology.Cellular and molecular neurobiology · 2017Review
- Liposomes modified with cardiolipin can act as a platform to regulate the potential flux of NADPMetabolic engineering communications · 2016Article
- Molecular dynamics simulations of creatine kinase and adenine nucleotide translocase in mitochondrial membrane patch.The Journal of biological chemistry · 2012Article
- Lipid antioxidants: free radical scavenging versus regulation of enzymatic lipid peroxidation.Journal of clinical biochemistry and nutrition · 2011Article
- Mitochondrial creatine kinase interaction with cardiolipin-containing biomimetic membranes is a two-step process involving adsorption and insertion.European biophysics journal : EBJ · 2010Article
- Cardiolipin membrane domains in prokaryotes and eukaryotes.Biochimica et biophysica acta · 2009Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is well established that the octameric mitochondrial form of creatine kinase (mtCK) binds to the outer face of the inner mitochondrial membrane mainly via electrostatic interactions with cardiolipin (CL). However, little is known about the consequences of these interactions on membrane and protein levels. Brewster angle microscopy investigations provide, for the first time to our knowledge, images indicating that mtCK binding induced cluster formation on CL monolayers. The thickness of the clusters (10-12 nm) corresponds to the theoretical height of the mtCK-CL complex. Protein insertion into a condensed CL film, together with monolayer stabilization after protein addition, was observed by means of differential capacity measurements. Polarization modulation infrared reflection-absorption spectroscopy showed that the mean orientation of alpha-helices within the protein shifted upon CL binding from 30 degrees to 45 degrees with respect to the interface plane, demonstrating protein domain movements. A comparison of data obtained with CL and phosphatidylcholine/phosphatidylethanolamine/CL (2:1:1) monolayers indicates that mtCK is able to selectively recruit CL molecules within the mixed monolayer, consolidating and changing the morphology of the interfacial film. Therefore, CL-rich domains induced by mtCK binding could modulate mitochondrial inner membrane morphology into a raft-like organization and influence essential steps of mitochondria-mediated apoptosis.
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