The Intermolecular Interaction between the PH Domain and the C-terminal Domain of Arabidopsis Dynamin-like 6 Determines Lipid Binding Specificity

Lee, Sunghoon; Jin, Jing Bo; Song, Jinhee; Min, Myung Ki; Park, Dae Sup; Kim, Yong-Woo; Hwang, Inhwan

doi:10.1074/jbc.m204770200

Cited by 29 publications

(28 citation statements)

References 53 publications

(95 reference statements)

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“…However, although PH domains can mediate membrane localization (18), and although previous studies demonstrated that the Spo71 PH domains can bind the phosphoinositide phosphatidylinositol 3-phosphate (PI3) promiscuously and with weak affinity (49), neither PH domain of Spo71 was sufficient to mediate membrane localization in vegetatively growing cells. It is important to note that our experiments showing that the PH domains are not sufficient for membrane localization do not rule out a relationship between SPO71's PH domains and phosphatidylinositol phosphates (PIPs), as other PH domain proteins have been shown to require regions outside the PH domain for the PH domain to correctly bind PIPs (17,39).…”

Section: Discussionmentioning

confidence: 99%

SPO71 Mediates Prospore Membrane Size and Maturation in Saccharomyces cerevisiae

et al. 2012

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The mechanisms that control the size and shape of membranes are not well understood, despite the importance of these structures in determining organelle and cell morphology. The prospore membrane, a double lipid bilayer that is synthesized de novo during sporulation in S. cerevisiae, grows to surround the four meiotic products. This membrane determines the shape of the newly formed spores and serves as the template for spore wall deposition. Ultimately, the inner leaflet of the prospore membrane will become the new plasma membrane of the cell upon germination. Here we show that Spo71, a pleckstrin homology domain protein whose expression is induced during sporulation, is critical for the appropriate growth of the prospore membrane. Without SPO71, prospore membranes surround the nuclei but are abnormally small, and spore wall deposition is disrupted. Sporulating spo71⌬ cells have prospore membranes that properly localize components to their growing leading edges yet cannot properly localize septin structures. We also found that SPO71 genetically interacts with SPO1, a gene with homology to the phospholipase B gene that has been previously implicated in determining the shape of the prospore membrane. Together, these results show that SPO71 plays a critical role in prospore membrane development. The membrane is an important determinant of the shape of biological structures (34). As both organelles and cells are bounded by lipid bilayers, membranes are instrumental in their morphology. However, the mechanisms that underlie the control of the size and shape of these limiting membranes are not fully understood.Diploid Saccharomyces cerevisiae cells undergo sporulation in response to a lack of nitrogen and fermentable carbon sources (reviewed in reference 26). During this process, the cell undergoes meiosis and remodels its interior as it packages the meiotic products into spores, the equivalent of its gametes. Four spores are formed within the mother cell, which becomes known as the ascus. Upon reintroduction of nutrients into the environment, these spores can either grow vegetatively as haploid cells or mate with cells of the opposite mating type to create diploid cells.The shape of these spores is determined by the prospore membrane (PSM), a double membrane that is synthesized de novo during sporulation by post-Golgi vesicle fusion at the spindle pole body. The PSM grows to surround the meiotic nuclei and undergoes a cytokinetic event to encapsulate each nucleus. The growth of the PSM must be regulated such that it grows to properly encapsulate nuclei and cytoplasmic material and matures into a spherical configuration (9, 40). Following completion of PSM development, the lumen of the double membrane expands and serves as the site of spore wall deposition. The spore wall, comprised of mannoprotein, ␤-glucan, chitosan, and dityrosine layers, differs from the vegetative cell wall in its composition and offers increased protection to environmental stresses (7). Midway through spore morphogenesis, the outer prospore memb...

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Section: Discussionmentioning

confidence: 99%

SPO71 Mediates Prospore Membrane Size and Maturation in Saccharomyces cerevisiae

et al. 2012

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“…The plant ADL6 dynamin, that binds adaptatin and actin, has a PI-3P specific PH domain (phosphoinositide recognition domain) and its mutation abolished the trafficking of vacuole proteins. ADL6 is therefore an important protein that connects PI-3P local concentration and sorting to the vacuole [54]. However, nothing is known about the lipid composition and the lipid selectivity of all these vesicles.…”

Section: Transfer To the Vacuolesmentioning

confidence: 99%

Glycerolipid transfer for the building of membranes in plant cells

Jouhet

Maréchal

Block

2007

Progress in Lipid Research

130

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“…5 Top, lanes 2 and 3). The binding of the ARC5 translation product to isolated chloroplasts may be effected in part by the PH domain, which has been shown to mediate lipid binding of other dynamin-like proteins (34,38). In contrast, two chloroplast-targeted control proteins, one localized to the inner envelope (Fig.…”

Section: Localization Of Arc5mentioning

confidence: 99%

ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery

Gao

Kadirjan-Kalbach

Froehlich

et al. 2003

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

250

254

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Chloroplast division in plant cells is orchestrated by a complex macromolecular machine with components positioned on both the inner and outer envelope surfaces. The only plastid division proteins identified to date are of endosymbiotic origin and are localized inside the organelle. Employing positional cloning methods in Arabidopsis in conjunction with a novel strategy for pinpointing the mutant locus, we have identified a gene encoding a new chloroplast division protein, ARC5. Mutants of ARC5 exhibit defects in chloroplast constriction, have enlarged, dumbbellshaped chloroplasts, and are rescued by a wild-type copy of ARC5. The ARC5 gene product shares similarity with the dynamin family of GTPases, which mediate endocytosis, mitochondrial division, and other organellar fission and fusion events in eukaryotes. Phylogenetic analysis showed that ARC5 is related to a group of dynamin-like proteins unique to plants. A GFP-ARC5 fusion protein localizes to a ring at the chloroplast division site. Chloroplast import and protease protection assays indicate that the ARC5 ring is positioned on the outer surface of the chloroplast. Thus, ARC5 is the first cytosolic component of the chloroplast division complex to be identified. ARC5 has no obvious counterparts in prokaryotes, suggesting that it evolved from a dynamin-related protein present in the eukaryotic ancestor of plants. These results indicate that the chloroplast division apparatus is of mixed evolutionary origin and that it shares structural and mechanistic similarities with both the cell division machinery of bacteria and the dynamin-mediated organellar fission machineries of eukaryotes.T he chloroplasts of plants and algae are widely believed to have evolved only once from a free-living cyanobacterial endosymbiont (1). Over evolutionary time, many of the genes once present in the endosymbiont have been transferred to the nuclear genome where they have acquired sequences encoding transit peptides that direct their gene products back to the chloroplast (1, 2). This scenario describes the origin of the five previously identified plastid division proteins in plants, all of which evolved from related cell division proteins in cyanobacteria, are encoded in the nucleus, and are localized inside the chloroplast. These include FtsZ1 and FtsZ2, tubulin-like proteins that localize to a ring at the site of plastid constriction (3-10), MinD and MinE, which regulate placement of the plastid division site (11-13), and ARTEMIS, which appears to mediate constriction of the envelope membranes (14).Despite localization of the previously identified plastid division proteins inside the chloroplasts in plant cells, ultrastructural studies have shown that plastid division entails the coordinated activity of components localized outside as well as inside the organelle. In plants, the chloroplast division complex comprises electron-dense structures situated both on the stromal surface of the inner envelope membrane and on the cytosolic surface of the outer membrane (15). These structur...

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The Intermolecular Interaction between the PH Domain and the C-terminal Domain of Arabidopsis Dynamin-like 6 Determines Lipid Binding Specificity

Cited by 29 publications

References 53 publications

SPO71 Mediates Prospore Membrane Size and Maturation in Saccharomyces cerevisiae

SPO71 Mediates Prospore Membrane Size and Maturation in Saccharomyces cerevisiae

Glycerolipid transfer for the building of membranes in plant cells

ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery

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