An Ankyrin Repeat Domain of AKR2 Drives Chloroplast Targeting through Coincident Binding of Two Chloroplast Lipids

Kim, Dae Heon; Park, Mi Jeong; Gwon, G.H.; Silkov, Antonina; Xu, Zheng; Yang, Eun Chan; Song, Seo-Hyeon; Song, Kyungyoung; Kim, Younghyun; Yoon, Hwan Su; Honig, Barry; Cho, Wonhwa; Cho, Yunje; Hwang, Inhwan

doi:10.1016/j.devcel.2014.07.026

Cited by 46 publications

(34 citation statements)

References 61 publications

(85 reference statements)

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“…PG, aside from its essential role in CL biosynthesis, also fulfills various functions in specific membranes of some eukaryotic organisms. For example, PG is the sole phospholipid of thylakoid membranes in eukaryotic oxygenic photosynthetic organisms [21,22] and it is an important component of pulmonary surfactant, an essential fluid produced by alveolar type II cells that covers the entire surface of the lung [23]. In yeast cells, PG is a low abundance phospholipid, even under the conditions of aerobic growth [6].…”

Section: Introductionmentioning

confidence: 99%

Specific degradation of phosphatidylglycerol is necessary for proper mitochondrial morphology and function

Pokorná

C̆ermáková

Horváth

et al. 2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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In yeast, phosphatidylglycerol (PG) is a minor phospholipid under standard conditions; it can be utilized for cardiolipin (CL) biosynthesis by CL synthase, Crd1p, or alternatively degraded by the phospholipase Pgc1p. The Saccharomyces cerevisiae deletion mutants crd1Δ and pgc1Δ both accumulate PG. Based on analyses of the phospholipid content of pgc1Δ and crd1Δ yeast, we revealed that in yeast mitochondria, two separate pools of PG are present, which differ in their fatty acid composition and accessibility for Pgc1p-catalyzed degradation. In contrast to CL-deficient crd1Δ yeast, the pgc1Δ mutant contains normal levels of CL. This makes the pgc1Δ strain a suitable model to study the effect of accumulation of PG per se. Using fluorescence microscopy, we show that accumulation of PG with normal levels of CL resulted in increased fragmentation of mitochondria, while in the absence of CL, accumulation of PG led to the formation of large mitochondrial sheets. We also show that pgc1Δ mitochondria exhibited increased respiration rates due to increased activity of cytochrome c oxidase. Taken together, our results indicate that not only a lack of anionic phospholipids, but also excess PG, or unbalanced ratios of anionic phospholipids in mitochondrial membranes, have harmful consequences on mitochondrial morphology and function.

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Section: Introductionmentioning

confidence: 99%

Specific degradation of phosphatidylglycerol is necessary for proper mitochondrial morphology and function

Pokorná

C̆ermáková

Horváth

et al. 2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…It remains unclear whether in plants a 'pre-targeting' factor(s) regulates the open-to-closed structural transition of ArsA1 prior to TA substrate binding. Several studies have suggested that OEP9 and Toc33/Toc34 interact with the cytosolic targeting factor AKR2 (Arabidopsis ankyrin repeat protein) (Bae et al, 2008;Dhanoa et al, 2010;Kim et al, 2014;Lee et al, 2014), but it is not known if AKR2 communicates with ArsA proteins prior to targeting TA proteins to the chloroplast outer membrane.…”

Section: Discussionmentioning

confidence: 99%

Structural analysis of chloroplast tail‐anchored membrane protein recognition by ArsA1

Lin

Chen

et al. 2019

The Plant Journal

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Summary In mammals and yeast, tail‐anchored (TA) membrane proteins destined for the post‐translational pathway are safely delivered to the endoplasmic reticulum (ER) membrane by a well‐known targeting factor, TRC40/Get3. In contrast, the underlying mechanism for translocation of TA proteins in plants remains obscure. How this unique eukaryotic membrane‐trafficking system correctly distinguishes different subsets of TA proteins destined for various organelles, including mitochondria, chloroplasts and the ER, is a key question of long standing. Here, we present crystal structures of algal ArsA1 (the Get3 homolog) in a distinct nucleotide‐free open state and bound to adenylyl‐imidodiphosphate. This approximately 80‐kDa protein possesses a monomeric architecture, with two ATPase domains in a single polypeptide chain. It is capable of binding chloroplast (TOC34 and TOC159) and mitochondrial (TOM7) TA proteins based on features of its transmembrane domain as well as the regions immediately before and after the transmembrane domain. Several helices located above the TA‐binding groove comprise the interlocking hook‐like motif implicated by mutational analyses in TA substrate recognition. Our data provide insights into the molecular basis of the highly specific selectivity of interactions of algal ArsA1 with the correct sets of TA substrates before membrane targeting in plant cells.

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“…Previously, we reported that the ARD of the transient receptor potential cation channel subfamily V member 4 (TRPV4) bound to PI(4,5)P 2 (Takahashi et al, ). The plant ARD protein ankyrin repeat‐containing protein 2 (AKR2) was also shown to bind to membrane (Kim et al, ). Furthermore, the ARDs of ankyrin repeat and KH domain‐containing protein 1 (ANKHD1) and of ankycorbin were shown to be involved in membrane deformation (Kitamata, Hanawa‐Suetsugu, Maruyama, & Suetsugu, ; Wolf et al, ).…”

Section: Introductionmentioning

confidence: 99%

The membrane binding and deformation property of vaccinia virus K1 ankyrin repeat domain protein

et al. 2020

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Membrane lipids are essential participants in cellular events, but only a small number of lipid‐interacting proteins have been characterized. Taking advantage of the small genome (~270 genes) of the vaccinia virus, we screened for soluble lipid‐binding proteins and found 27 proteins to be soluble after expression in Escherichia coli. Among them, 4 proteins were found to strongly bind to the total bovine brain lipid extract (Folch I fraction) that contained large amounts of phosphatidylserine in vitro. Out of the 4 proteins, 3 were unique proteins to viruses. Another protein, K1, solely contained an ankyrin repeat domain (ARD). ARD is conserved in large numbers of proteins in bacteria, archaea, eukaryotes and viruses, suggesting the possibilities of the membrane binding of ARDs in varieties of proteins. Furthermore, K1 deformed the lipid membrane dependently on the charged lipids. The tubulation and membrane binding was enhanced with increased negative membrane charge from phosphatidylinositol 4,5‐bisphosphate (PI(4,5)P2). The basic amino acid residues in the ARD were essential for membrane deformation, suggesting electrostatic interactions between K1 and the membrane for membrane deformation.

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An Ankyrin Repeat Domain of AKR2 Drives Chloroplast Targeting through Coincident Binding of Two Chloroplast Lipids

Cited by 46 publications

References 61 publications

Specific degradation of phosphatidylglycerol is necessary for proper mitochondrial morphology and function

Specific degradation of phosphatidylglycerol is necessary for proper mitochondrial morphology and function

Structural analysis of chloroplast tail‐anchored membrane protein recognition by ArsA1

The membrane binding and deformation property of vaccinia virus K1 ankyrin repeat domain protein

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