Dolichyl phosphate induces non-bilayer structures, vesicle fusion and transbilayer movement of lipids: a model membrane study

Duijn, G. Van; Valtersson, Conny; Chojnacki, Tadeusz; Verkleij, Arie J.; Dallner, Gustav; Kruijff, Ben de

doi:10.1016/0005-2736(86)90423-2

Cited by 98 publications

(37 citation statements)

References 44 publications

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“…The experiments show that dolichol and dolichol analogues exert a considerable influence on the organization and packing Table 2. Dolichol distribution in human and rat organs of phospholipids [23][24][25][26][27][28]. Polyisoprenoids appear to increase the fluidity of phospholipids in bilayers, destabilize lipid membranes, elicit formation of inverted micelles within the membrane (HII phase and lipidic particles) and increase permeability.…”

Section: Functions Of Dolicholmentioning

confidence: 99%

“…Polyisoprenoids appear to increase the fluidity of phospholipids in bilayers, destabilize lipid membranes, elicit formation of inverted micelles within the membrane (HII phase and lipidic particles) and increase permeability. Most interesting are the findings that dolichol enhances vesicle fusion in a concentration-dependent manner and that dolichyl phosphate stimulates the fusion of rat liver microsomes and unilamellar lipid vesicles [29]. In this way dolichol in membranes may play an important role in the extensive membrane traffic between the Golgi system, the plasma membrane and the lysosomes, which is the basis for many important events in cellular life.…”

Section: Functions Of Dolicholmentioning

confidence: 99%

“…centre of the membrane, but in this case the phosphate group is located at the outer surface and the oc-terminal end of the polyisoprene runs parallel with the fatty acid chains [27].…”

Section: Functions Of Dolicholmentioning

confidence: 99%

See 2 more Smart Citations

The biological role of dolichol

Chojnacki

Dallner²

1988

Biochemical Journal

286

191

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Section: Functions Of Dolicholmentioning

confidence: 99%

Section: Functions Of Dolicholmentioning

confidence: 99%

See 1 more Smart Citation

The biological role of dolichol

Chojnacki

Dallner²

1988

Biochemical Journal

286

191

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“…Prior studies on polyprenol-dependent pathways have principally focused on redacted experimental systems representing two of the three key variables. For example, the effect of varying the substrate polyprenol groups has been studied using glycan assembly enzymes that have been solubilized from the native lipid bilayer with detergent (16)(17)(18); and interactions of polyprenyl-linked compounds with model membrane systems, such as liposomes, in the absence of membrane-bound proteins have been investigated using biophysical techniques, including computational modeling and NMR spectroscopy (19)(20)(21)(22)(23)(24).…”

mentioning

confidence: 99%

Lipid bilayer nanodisc platform for investigating polyprenol-dependent enzyme interactions and activities

Hartley

Schneggenburger

Imperiali

2013

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

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Membrane-bound polyprenol-dependent pathways are important for the assembly of essential glycoconjugates in all domains of life. However, despite their prevalence, the functional significance of the extended linear polyprenyl groups in the interactions of the glycan substrates, the biosynthetic enzymes that act upon them, and the membrane bilayer in which they are embedded remains a mystery. These interactions are investigated simultaneously and uniquely through application of the nanodisc membrane technology. The Campylobacter jejuni N-linked glycosylation pathway has been chosen as a model pathway in which all of the enzymes and substrates are biochemically accessible. We present the functional reconstitution of two enzymes responsible for the early membrane-committed steps in glycan assembly. Protein stoichiometry analysis, fluorescence-based approaches, and biochemical activity assays are used to demonstrate the colocalization of the two enzymes in nanodiscs. Isotopic labeling of the substrates reveals that undecaprenyl-phosphate is coincorporated into discs with the two enzymes, and furthermore, that both enzymes are functionally reconstituted and can sequentially convert the coembedded undecaprenyl-phosphate into undecaprenyl-diphosphate-linked disaccharide. These studies provide a proof-of-concept demonstrating that the nanodisc model membrane system represents a promising experimental platform for analyzing the multifaceted interactions among the enzymes involved in polyprenol-dependent glycan assembly pathways, the membrane-associated substrates, and the lipid bilayer. The stage is now set for exploration of the roles of the conserved polyprenols in promoting protein-protein interactions among pathway enzymes and processing of substrates through sequential steps in membrane-associated glycan assembly.

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“…Several biophysical studies have revealed that the presence of polyprenyl-phosphate or its derivatives (polyprenol, polyprenyl-diphosphate, or polyprenyl-sugar) in model membrane vesicles significantly increases their fluidity and ion permeability. 109,112,117 It is reasonable to figure out that local destabilization of the membrane may, thus, be a determinant to overcome the translocation energetic barrier.…”

mentioning

confidence: 99%

Deciphering the Metabolism of Undecaprenyl-Phosphate: The Bacterial Cell-Wall Unit Carrier at the Membrane Frontier

Manat

Roure

Auger

et al. 2014

Microbial Drug Resistance

121

139

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During the biogenesis of bacterial cell-wall polysaccharides, such as peptidoglycan, cytoplasmic synthesized precursors should be trafficked across the plasma membrane. This essential process requires a dedicated lipid, undecaprenyl-phosphate that is used as a glycan lipid carrier. The sugar is linked to the lipid carrier at the inner face of the membrane and is translocated toward the periplasm, where the glycan moiety is transferred to the growing polymer. Undecaprenyl-phosphate originates from the dephosphorylation of its precursor undecaprenyl-diphosphate, with itself generated by de novo synthesis or by recycling after the final glycan transfer. Undecaprenyl-diphosphate is de novo synthesized by the cytosolic cis-prenyltransferase undecaprenyldiphosphate synthase, which has been structurally and mechanistically characterized in great detail highlighting the condensation process. In contrast, the next step toward the formation of the lipid carrier, the dephosphorylation step, which has been overlooked for many years, has only started revealing surprising features. In contrast to the previous step, two unrelated families of integral membrane proteins exhibit undecaprenyldiphosphate phosphatase activity: BacA and members of the phosphatidic acid phosphatase type 2 super-family, raising the question of the significance of this multiplicity. Moreover, these enzymes establish an unexpected link between the synthesis of bacterial cell-wall polymers and other biological processes. In the present review, the current knowledge in the field of the bacterial lipid carrier, its mechanism of action, biogenesis, recycling, regulation, and future perspective works are presented.

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Dolichyl phosphate induces non-bilayer structures, vesicle fusion and transbilayer movement of lipids: a model membrane study

Cited by 98 publications

References 44 publications

The biological role of dolichol

The biological role of dolichol

Lipid bilayer nanodisc platform for investigating polyprenol-dependent enzyme interactions and activities

Deciphering the Metabolism of Undecaprenyl-Phosphate: The Bacterial Cell-Wall Unit Carrier at the Membrane Frontier

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