GTP hydrolysis by transitional endoplasmic reticulum from rat liver inhibited by all-trans-retinol

Zhao, Jiemin; Morré, D. James; Paulik, Mark; Yim, J.; Morré, Dorothy M.

doi:10.1016/0167-4889(90)90037-e

Cited by 7 publications

(3 citation statements)

References 6 publications

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“…The first of these was a retinol-inhibited GTPase of unknown function which might function as a guanine nucleotide exchange protein or as a GTPase (Zhao et al 1990). The other was a retinol-modulated NADH: protein disulfide reductase (NADH oxidase) protein with protein disulfide-thiol interchange activity (Morré et al 1998).…”

Section: Retinol Stimulation Of Vesicle Budding In Rat Livermentioning

confidence: 98%

Cell-free analysis of Golgi apparatus membrane traffic in rat liver

Dj¹

1998

Histochemistry and Cell Biology

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Cell-free systems for the analysis of Golgi apparatus membrane traffic rely either on highly purified cell fractions or analysis by specific trafficking markers or both. Our work has employed a cell-free transfer system from rat liver based on purified fractions. Transfer of any constituent present in the donor fraction that can be labeled (protein, phospholipid, neutral lipid, sterol, or glycoconjugate) may be investigated in a manner not requiring a processing assay. Transition vesicles were purified and Golgi apparatus cisternae were subfractionated by means of preparative free-flow electrophoresis. Using these transition vesicles and Golgi apparatus subfractions, transfer between transitional endoplasmic reticulum and cis Golgi apparatus was investigated and the process subdivided into vesicle formation and vesicle fusion steps. In liver, vesicle formation exhibited both ATP-independent and ATP-dependent components whereas vesicle fusion was ATP-independent. The ATP-dependent component of transfer was donor and acceptor specific and appeared to be largely unidirectional, i.e., ATP-dependent retrograde (cis Golgi apparatus to transitional endoplasmic reticulum) traffic was not observed. ATP-dependent transfer in the liver system and coatomer-driven ATP-independent transfer in more refined yeast and cultured cell systems are compared and discussed in regard to the liver system. A model mechanism developed for ATP-dependent budding is proposed where a retinol-stimulated and brefeldin A-inhibited NADH protein disulfide oxidoreductase (NADH oxidase) with protein disulfide-thiol interchange activity and an ATP-requiring protein capable of driving physical membrane displacement are involved. It has been suggested that this mechanism drives both the cell enlargement and the vesicle budding that may be associated with the dynamic flow of membranes along the endoplasmic reticulum-vesicle-Golgi apparatus-plasma membrane pathway.

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Section: Retinol Stimulation Of Vesicle Budding In Rat Livermentioning

confidence: 98%

Cell-free analysis of Golgi apparatus membrane traffic in rat liver

Dj¹

1998

Histochemistry and Cell Biology

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“…When different nucleotide triphosphates were employed in the cell-free system to study the nucleotide triphosphate dependence, transition vesicle formarion specifically required ATP (M. Panlik and D. J. MorrO, unpublished results). Subsequently a Mg2+-ATPase activity was observed in the TER and was shown by ion-exchange chromatography to be distinct from proteins associated with IDPase and GTPase activities (Zhao et al, 1990). Here we report the characterization, isolation and amino acid sequence of the ATPase from the TER which appears to represent a functional component of the ATP-responsive vesicle budding ~om the TER.…”

mentioning

confidence: 99%

Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver.

Zhang

Ashendel

Becker

et al. 1994

The Journal of Cell Biology

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Abstract. The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from partrough, part-smooth transitional elements of the endoplasmic reticulum (TER). Vesicle budding from the TER is an ATP-dependent process both in vivo and in vitro. An ATPase with a monomer molecular weight of 100 kD by SDS-PAGE has been isolated from TER and designated as TER ATPase. The native TER ATPase has been characterized as a hexamer of six 100-kD subunits by gel filtration. The protein catalyzes the hydrolysis of [732-P]ATP and is phosphorylated in the presence of Mg 2÷. It is distinct from the classical transport ATPases based on pH optima, ion effects, and inhibitor specificity. Electron microscopy of negatively stained preparations revealed the TER ATPase to be a ring-shaped structure with sixfold rotational symmetry. A 19-amino acid sequence of TER ATPase having 84 % identity with valosincontaining protein and 64% identity with a yeast cellcycle control protein CDC48p was obtained. Antisynthetic peptide antisera to a 15-amino acid portion of the sequence of TER ATPase recognized a 100-kD protein from TER. These antisera reduced the ATPdependent cell-free formation of transition vesicles from isolated TER of rat liver. In a reconstituted membrane transfer system, TER ATPase antisera inhibited transfer of radiolabeled material from endoplasmic reticulum to Golgi apparatus, while preimmune sera did not. The results suggest that the TER ATPase is obligatorily involved in the ATP requirements for budding of transition vesicles from the TER. cDNA clones encoding TER ATPase were isolated by immunoscreening a rat liver cDNA library with the afffinity-purified TER ATPase antibody. A computer search of deduced amino acid sequences revealed the cloned TER ATPase to be the rat equivalent of porcine valosin-containing protein, a member of a novel family of ATP binding, homo-oligomeric proteins including the N-ethylmaleimide-sensitive fusion protein.

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“…It was supposed that the amount of 1 × 10 8 RA molecules (as in our experimental setting) could not exclusively induce such profound morphological changes in the GA, preserving all other intracellular organelles, if "simple" fluidity alteration of the intracellular membranes took place. It was further supposed that the observed-RA effects may occur in an RAR-independent way that involves protein kinases and second messenger cascades (Anderson et al, 1985;Cope and Boutwell, 1985;Cope, 1986;Nowack et al, 1990;Zhao et al, 1990;Evain-Brion et al, 1991;Tang and Ziboh, 1991;Kurie et al, 1993;Bouzinba-Segard et al, 1994;Kahl-Rainer and Marian, 1994;Carter et al, 1998;Morré et al, 1998). The experimental evidence that the RAinduced GA-transformation could be suppressed by exposure to phorbol ester supported this assumption, and clearly demonstrated that some components of the protein kinase C (PKC) cascade play an important role in the RA-induced GA disruption.…”

Section: Discussionmentioning

confidence: 99%

Retinoic Acid-Induced Golgi Apparatus Disruption in F2000 Fibroblasts: A Model for Enhanced Intracellular Retrograde Transport

Tzankov¹

2003

BMB Reports

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Retinoic acid (RA) can transform the Golgi apparatus (GA) into a diffuse vacuolar aggregate and increase the toxicity of some immunotoxins that enter into cells by receptor-mediated endocytosis. An ultramorphological study of the RA-induced GA disruption was performed on F2000 fibroblasts. Cultures were treated with 0.11 to 30 µM RA for 7 -180 min. The endocytosis of Limax flavus agglutinin-peroxidase conjugate (LFA), and the interactions between a phorbol ester (PMA) and RA concerning GA disruption, were examined. Exposure to 0.33 µM RA for 20 min transformed the GA into vacuolar aggregate. These vacuoles were not involved in endocytosis since they remained unstained after endocytosis of LFA. However, the lysosomes were involved in endocytosis, as they were strongly stained. Therefore, a RA-induced shift towards lysosomal routing of the entered LFA was presumed. Exposure to PMA made cells resistant to the Golgi-disturbing effects of RA, indicating that protein kinase C plays an important role in this process.

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GTP hydrolysis by transitional endoplasmic reticulum from rat liver inhibited by all-trans-retinol

Cited by 7 publications

References 6 publications

Cell-free analysis of Golgi apparatus membrane traffic in rat liver

Cell-free analysis of Golgi apparatus membrane traffic in rat liver

Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver.

Retinoic Acid-Induced Golgi Apparatus Disruption in F2000 Fibroblasts: A Model for Enhanced Intracellular Retrograde Transport

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