2018
DOI: 10.1371/journal.pone.0206355
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Identification and characterization of protein N-myristoylation occurring on four human mitochondrial proteins, SAMM50, TOMM40, MIC19, and MIC25

Abstract: Previously, we showed that SAMM50, a mitochondrial outer membrane protein, is N-myristoylated, and this lipid modification is required for the proper targeting of SAMM50 to mitochondria. In this study, we characterized protein N-myristoylation occurring on four human mitochondrial proteins, SAMM50, TOMM40, MIC19, and MIC25, three of which are components of the mitochondrial intermembrane space bridging (MIB) complex, which plays a critical role in the structure and function of mitochondria. In vitro and in viv… Show more

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Cited by 23 publications
(35 citation statements)
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“…These include NADH-cytochrome b5 reductase, Sam50 (a sorting and assembly machinery complex component), MOSC1/2 through co-translational MYR [61], and several posttranslationally MYRed proteins (see below). TOM40 is a MYRed subunit of the mitochondrial import receptor subunit lying within the OMM but with an N-terminus protruding at the outer side [62,63]. It was unexpected that MYRed proteins could exist within the intermembrane space, including the MIC19 and MIC25 components of the mitochondrial contact site complex (MICOS, also found in yeast; Table 1), which is crucial for maintaining crista integrity and mitochondrial function [64], and other proteins of the inner membrane space such as complex I subunits of the respiratory chain including B18/NDUFB7 and NDUF4 [7].…”
Section: Mitochondriamentioning
confidence: 99%
“…These include NADH-cytochrome b5 reductase, Sam50 (a sorting and assembly machinery complex component), MOSC1/2 through co-translational MYR [61], and several posttranslationally MYRed proteins (see below). TOM40 is a MYRed subunit of the mitochondrial import receptor subunit lying within the OMM but with an N-terminus protruding at the outer side [62,63]. It was unexpected that MYRed proteins could exist within the intermembrane space, including the MIC19 and MIC25 components of the mitochondrial contact site complex (MICOS, also found in yeast; Table 1), which is crucial for maintaining crista integrity and mitochondrial function [64], and other proteins of the inner membrane space such as complex I subunits of the respiratory chain including B18/NDUFB7 and NDUF4 [7].…”
Section: Mitochondriamentioning
confidence: 99%
“…The cell lysates labeled with Alk-Myr (46 μL) were treated with 4 μL of freshly premixed click chemistry reaction cocktail [1 μL Az-TAMRA (5 mM), 1 μL TCEP (50 mM), 1 μL TBTA (5 mM), and 1 μL CuSO 4 ·5H 2 O (50 mM)] in a total reaction volume of 50 μL for 1 h at room temperature [21]. After copper(I)-catalyzed azide–alkyne cycloaddition (CuAAC), 500 μL of MeOH was added to the sample, which was then kept at –80°C overnight.…”
Section: Methodsmentioning
confidence: 99%
“…The membrane was probed with an nti-FLAG antibody. Immunoreactive proteins were detected specifically by incubation with protein G-HRP conjugate or HRP-conjugated anti-mouse IgG as previously described [19,21].…”
Section: Methodsmentioning
confidence: 99%
“…In addition, some proteins must undergo N-myristoylation for subcellular trafficking and localization. Some mitochondria-related proteins, such as TOMM40, SAMM50 [ 32 ] and, CLPABP [ 33 ], were demonstrated to require the function of myristoylated proteins to bind to the mitochondrial outer membrane. In one mechanism, the hydrophobic myristoyl group motif increases dependence of the protein to reduce cytoplasmic shuttling.…”
Section: Cross Talk Among the Physiological Functional Components Of mentioning
confidence: 99%