Dynamin-related proteins Vps1p and Dnm1p control peroxisome abundance in<i>Saccharomyces cerevisiae</i>

Kuravi, Kasinath; Nagotu, Shirisha; Krikken, Arjen M; Sjollema, Klaas; Deckers, Markus; Erdmann, Ralf; Veenhuis, Marten; Klei, Ida J. van der

doi:10.1242/jcs.03166

Cited by 185 publications

(207 citation statements)

References 44 publications

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“…However, deletion of DNM1 affects the division of peroxisomes only in oleic acid, and the defect is not as strong as that of the vps1Δ mutant. 16 Consistent with these results, pexophagy was significantly blocked in a vps1Δ strain, whereas there was only an intermediate effect in the dnm1Δ mutant (Fig. 1B and D).…”

Section: Discussionsupporting

confidence: 87%

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The progression of peroxisomal degradation through autophagy requires peroxisomal division

et al. 2014

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Section: Discussionsupporting

confidence: 87%

“…1B and C), which is consistent with the previous report that the replication of peroxisomes is compromised in these mutants. 16 In vps1Δ and dnm1Δ vps1Δ mutants, the peroxisomes were highly clustered making it difficult to differentiate and quantify individual peroxisomes (Fig. 1B).…”

Section: Peroxisomal Fission Is a Significant Step During Pexophagymentioning

confidence: 99%

The progression of peroxisomal degradation through autophagy requires peroxisomal division

et al. 2014

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“…(Opisthokont vesicle dynamins do not form a robust clade, so we cannot rule out separate duplications in fungi and metazoans.) Independent observations support this multiple-duplication scenario: The PH domains of plant and metazoan classical vesicle dynamins appear to have independent origins (33); the mitochondrial and vesicle dynamins of alveolates are suggested to be related (34); and the mitochondrial and vesicle dynamins in yeast (Dnm1 and Vps1) share a role in peroxisomal division (35), indicating a recent divergence. Following duplication, the mitochondrial variant retains most of its ancestral signature (AAAAAAAA; Fig.…”

Section: Leca Had a Bifunctional Dynamin That Duplicated Multiple Indmentioning

confidence: 97%

Ancient dynamin segments capture early stages of host–mitochondrial integration

Purkanti

Thattai

2015

Proc. Natl. Acad. Sci. U.S.A.

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Eukaryotic cells use dynamins-mechano-chemical GTPases-to drive the division of endosymbiotic organelles. Here we probe early steps of mitochondrial and chloroplast endosymbiosis by tracing the evolution of dynamins. We develop a parsimony-based phylogenetic method for protein sequence reconstruction, with deep time resolution. Using this, we demonstrate that dynamins diversify through the punctuated transformation of sequence segments on the scale of secondary-structural elements. We find examples of segments that have remained essentially unchanged from the 1.8-billion-y-old last eukaryotic common ancestor to the present day. Stitching these together, we reconstruct three ancestral dynamins: The first is nearly identical to the ubiquitous mitochondrial division dynamins of extant eukaryotes, the second is partially preserved in the myxovirus-resistance-like dynamins of metazoans, and the third gives rise to the cytokinetic dynamins of amoebozoans and plants and to chloroplast division dynamins. The reconstructed sequences, combined with evolutionary models and published functional data, suggest that the ancestral mitochondrial division dynamin also mediated vesicle scission. This bifunctional protein duplicated into specialized mitochondrial and vesicle variants at least three independent times-in alveolates, green algae, and the ancestor of fungi and metazoans-accompanied by the loss of the ancient prokaryotic mitochondrial division protein FtsZ. Remarkably, many extant species that retain FtsZ also retain the predicted ancestral bifunctional dynamin. The mitochondrial division apparatus of such organisms, including amoebozoans, red algae, and stramenopiles, seems preserved in a nearprimordial form.eukaryote evolution | mitochondria | vesicles | dynamin | FtsZ E ukaryotes arose through the acquisition of mitochondria by an archaeal host cell about 2 billion y ago (1, 2), a watershed moment in the evolution of the modern compartmentalized cell plan (3). A second transformative endosymbiotic event, the acquisition of a cyanobacterium by a eukaryotic host to form chloroplasts, gave rise to the photosynthetic eukaryotic lineages (4). As the endosymbionts became integrated with their hosts, their growth and division became regulated by host-cellular machinery (5). Proteins of the dynamin superfamily were central to this process: Mitochondria and chloroplasts originally divided using a constricting ring of the prokaryotic cytoskeletal protein FtsZ, but dynamins have been recruited to these roles in all extant eukaryotes (6, 7). By reconstructing the evolutionary history of dynamins, we can probe the process of endosymbiont integration.The dynamin superfamily is diverse (8, 9), and different dynamin variants remodel membranes at different cellular locations (Table S1 and primary references therein). A major class of dynamins is essential for mitochondrial and peroxisomal division. Another large group drives the scission of clathrin-coated vesicles in organisms such as fungi and alveolates. A related group, the socal...

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“…The sequence of all PCR-generated fragments was verified by automated sequencing (MWG Biotech, Ebersberg, Germany). To clone pMDE24/2, DsRed.T1 was amplified from pMDE21 (37) by using PCR primers RE1685/1686 and inserted into pMDE23 (38) after SacI/SpeI digestion (pMDE24/1). Following SacI/ KpnI digestion of pMDE24/1, the entire MET25 PromDsRed.T1-Ant1-CYC1…”

Section: Methodsmentioning

confidence: 99%

The N-domain of Pex22p Can Functionally Replace the Pex3p N-domain in Targeting and Peroxisome Formation

Halbach

Rucktäschel

Rottensteiner

et al. 2009

Journal of Biological Chemistry

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Pex3p is a central component of the import machinery for peroxisomal membrane proteins (PMPs) that can reach peroxisomes via the endoplasmic reticulum (ER) and even trigger de novo peroxisome formation from the ER. Pex19p is the import receptor for type I PMPs, whereas targeting of type II PMPs, of which Pex3p so far represents the only species, does not require Pex19p. Pex3p possesses two domains with distinct function: a short N-terminal domain, which harbors the information for peroxisomal (and ER) targeting, and a C-terminal domain, which faces the cytosol and serves as a docking site for Pex19p, thereby delivering newly synthesized PMPs to the peroxisome. Here we show that the N-terminal domain of Pex3p can be functionally replaced by the N-terminal peroxisomal membrane targeting signal (mPTS) of Pex22p, a supposedly unrelated component of the import machinery for peroxisomal matrix proteins. An exchange of the mPTS of Pex22p by that of Pex3p likewise fully preserved the function of Pex22p. Neither of the two mPTS interacted with Pex19p, and in the absence of Pex19p, colocalization of Pex3p and Pex22p was observed, indicating that also Pex22p is targeted to peroxisomes by a type II mPTS. When a type I mPTS was hooked to the C-terminal domains of Pex22p and Pex3p, function was retained in the case of Pex22p and in part even for Pex3p. The C-terminal domain of Pex3p thus contains the relevant information required for de novo peroxisome formation, thereby challenging the concept of the N terminus of Pex3p being key in that process.Peroxisome biogenesis requires a set of proteins called peroxins, most of which accomplish the faithful import of matrix proteins (1-3). Two types of targeting signals are known to direct proteins to the peroxisomal lumen: a C-terminal peroxisomal targeting signal type 1 (PTS1) 2 comprising the C-terminal tripeptide SKL and conservative variants thereof, and an N-terminal PTS2. The import of peroxisomal membrane proteins (PMPs) follows a distinct route and depends on Pex3p and Pex19p in all of the species analyzed (4) and on Pex16p in mammals (5, 6).The majority of PMPs are recognized by Pex19p during or early after synthesis in the cytosol. Pex19p binding not only protects these hydrophobic proteins from aggregation but also delivers them to the peroxisomal membrane (7-10). Docking of the cargo-loaded Pex19p receptor at the peroxisomal membrane occurs via the C-terminal cytoplasmic domain of Pex3p (10 -13). In a subsequent, poorly understood step, PMPs are released from Pex19p for insertion into the peroxisomal membrane. Although some controversy exists in the literature on the nature of a peroxisomal membrane protein targeting signal (mPTS), it requires one or more transmembrane spans and a targeting-specific sequence that is identical to the Pex19p-binding site in at least a subset of PMPs (4, 10, 11).In mutants with a specific block in matrix protein import, PMPs are normally imported into so-called peroxisomal remnants. In contrast, in the absence of the peroxins required for PM...

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Dynamin-related proteins Vps1p and Dnm1p control peroxisome abundance inSaccharomyces cerevisiae

Cited by 185 publications

References 44 publications

The progression of peroxisomal degradation through autophagy requires peroxisomal division

The progression of peroxisomal degradation through autophagy requires peroxisomal division

Ancient dynamin segments capture early stages of host–mitochondrial integration

The N-domain of Pex22p Can Functionally Replace the Pex3p N-domain in Targeting and Peroxisome Formation

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