Transitional endoplasmic reticulum ATPase

2008 ◽  
Author(s):  
Florian Salomons
Keyword(s):  
Endoplasmic Reticulum ◽  
Transitional Endoplasmic Reticulum

Identification of Palmitoylated Transitional Endoplasmic Reticulum ATPase by Proteomic Technique and Pan Antipalmitoylation Antibody

2016 ◽  
Vol 15 (3) ◽  
pp. 956-962 ◽  
Author(s):  
Caiyun Fang ◽  
Xiaoqin Zhang ◽  
Lei Zhang ◽  
Xing Gao ◽  
Pengyuan Yang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Transitional Endoplasmic Reticulum

Response of a protein disulfide isomerase-like activity of transitional endoplasmic reticulum to all-trans retinol

Life Sciences ◽  
1996 ◽  
Vol 59 (4) ◽  
pp. 273-284 ◽  
Author(s):  
Elizabeth Jacobs ◽  
D.James Morré ◽  
Rafael de Cabo ◽  
Mark Sweeting ◽  
Dorothy M. Morré
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Transitional Endoplasmic Reticulum ◽  
Protein Disulfide

Molecular basis for low temperature compartment formation by transitional endoplasmic reticulum of rat liver

FEBS Letters ◽  
1992 ◽  
Vol 310 (3) ◽  
pp. 223-228 ◽  
Author(s):  
Patrick Moreau ◽  
Hélène Juguelin ◽  
Claude Cassagne ◽  
D.James Morré
Keyword(s):  
Endoplasmic Reticulum ◽  
Low Temperature ◽  
Rat Liver ◽  
Molecular Basis ◽  
Transitional Endoplasmic Reticulum

scholarly journals mRNA Localization and ER-based Protein Sorting Mechanisms Dictate the Use of Transitional Endoplasmic Reticulum-Golgi Units Involved in Gurken Transport in Drosophila Oocytes

2004 ◽  
Vol 15 (12) ◽  
pp. 5306-5317 ◽  
Author(s):  
Bram Herpers ◽  
Catherine Rabouille
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Transport ◽  
Transforming Growth Factor ◽  
Mrna Localization ◽  
Transforming Growth Factor Α ◽  
Transitional Endoplasmic Reticulum ◽  
Polarized Cells ◽  
Immuno Electron Microscopy ◽  
Factor Α ◽  
Exocytic Pathway

The anteroposterior and dorsoventral axes of the future embryo are specified within Drosophila oocytes by localizing gurken mRNA, which targets the secreted Gurken transforming growth factor-α synthesis and transport to the same site. A key question is whether gurken mRNA is targeted to a specialized exocytic pathway to achieve the polar deposition of the protein. Here, we show, by (immuno)electron microscopy that the exocytic pathway in stage 9–10 Drosophila oocytes comprises a thousand evenly distributed transitional endoplasmic reticulum (tER)-Golgi units. Using Drosophila mutants, we show that it is the localization of gurken mRNA coupled to efficient sorting of Gurken out of the ER that determines which of the numerous equivalent tER-Golgi units are used for the protein transport and processing. The choice of tER-Golgi units by mRNA localization makes them independent of each other and represents a nonconventional way, by which the oocyte implements polarized deposition of transmembrane/secreted proteins. We propose that this pretranslational mechanism could be a general way for targeted secretion in polarized cells, such as neurons.

scholarly journals Role of p97 and Syntaxin 5 in the Assembly of Transitional Endoplasmic Reticulum

2000 ◽  
Vol 11 (8) ◽  
pp. 2529-2542 ◽  
Author(s):  
Line Roy ◽  
John J.M. Bergeron ◽  
Christine Lavoie ◽  
Rob Hendriks ◽  
Jennifer Gushue ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Secretory Pathway ◽  
Atp Hydrolysis ◽  
Smooth Endoplasmic Reticulum ◽  
Atp Depletion ◽  
Low Density ◽  
Transitional Endoplasmic Reticulum ◽  
Membrane Compartment ◽  
A Cell

Transitional endoplasmic reticulum (tER) consists of confluent rough and smooth endoplasmic reticulum (ER) domains. In a cell-free incubation system, low-density microsomes (1.17 g cc− 1) isolated from rat liver homogenates reconstitute tER by Mg2+GTP- and Mg2+ATP-hydrolysis–dependent membrane fusion. The ATPases associated with different cellular activities protein p97 has been identified as the relevant ATPase. The ATP depletion by hexokinase or treatment with either N-ethylmaleimide or anti-p97 prevented assembly of the smooth ER domain of tER. High-salt washing of low-density microsomes inhibited assembly of the smooth ER domain of tER, whereas the readdition of purified p97 with associated p47 promoted reconstitution. The t-SNARE syntaxin 5 was observed within the smooth ER domain of tER, and antisyntaxin 5 abrogated formation of this same membrane compartment. Thus, p97 and syntaxin 5 regulate assembly of the smooth ER domain of tER and hence one of the earliest membrane differentiated components of the secretory pathway.

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