Identification of a gene required for membrane protein retention in the early secretory pathway.
about
The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesisEndoplasmic reticulum localization of Sec12p is achieved by two mechanisms: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain.Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae.Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomerRer1p as common machinery for the endoplasmic reticulum localization of membrane proteins.Transport through the yeast endocytic pathway occurs through morphologically distinct compartments and requires an active secretory pathway and Sec18p/N-ethylmaleimide-sensitive fusion protein.The Escherichia coli homologue of yeast RER2, a key enzyme of dolichol synthesis, is essential for carrier lipid formation in bacterial cell wall synthesisYeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis.Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites.Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis.Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations.Membrane trafficking in the yeast Saccharomyces cerevisiae modelSec12 binds to Sec16 at transitional ER sitesRequirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiaeA dominant negative mutant of sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells.NBD-labeled phosphatidylcholine and phosphatidylethanolamine are internalized by transbilayer transport across the yeast plasma membrane.Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells.TorsinA and the torsinA-interacting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast.Structure, mechanism and function of prenyltransferases.Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.The antibiotic gentamicin inhibits specific protein trafficking functions of the Arf1/2 family of GTPases.The fission yeast spo14+ gene encoding a functional homologue of budding yeast Sec12 is required for the development of forespore membranes.Drosophila KDEL receptor function in the embryonic salivary gland and epidermis.Large-scale evolutionary analyses on SecB subunits of bacterial sec system.Genetic analysis of intracellular aminoglycerophospholipid traffic.Identification of yeast genes involved in k homeostasis: loss of membrane traffic genes affects k uptake.Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeastRetention in endoplasmic reticulum 1 (RER1) modulates amyloid-β (Aβ) production by altering trafficking of γ-secretase and amyloid precursor protein (APP).Anchors aweigh: protein localization and transport mediated by transmembrane domainsIsoform-selective oligomer formation of Saccharomyces cerevisiae p24 family proteins.Secretory protein biogenesis and traffic in the early secretory pathwayTranscriptional regulation of secretory capacity by bZip transcription factors.Identification of potential regulatory elements for the transport of Emp24pRemodeling of ER-exit sites initiates a membrane supply pathway for autophagosome biogenesis.Multiple roles of Arf1 GTPase in the yeast exocytic and endocytic pathways.Rer1p competes with APH-1 for binding to nicastrin and regulates gamma-secretase complex assembly in the early secretory pathway.Rer1p, a retrieval receptor for ER membrane proteins, recognizes transmembrane domains in multiple modes.The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus.Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies.Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the golgi.
P2860
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P2860
Identification of a gene required for membrane protein retention in the early secretory pathway.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Identification of a gene requi ...... n the early secretory pathway.
@ast
Identification of a gene requi ...... n the early secretory pathway.
@en
type
label
Identification of a gene requi ...... n the early secretory pathway.
@ast
Identification of a gene requi ...... n the early secretory pathway.
@en
prefLabel
Identification of a gene requi ...... n the early secretory pathway.
@ast
Identification of a gene requi ...... n the early secretory pathway.
@en
P2860
P356
P1476
Identification of a gene requi ...... in the early secretory pathway
@en
P2093
S Nishikawa
P2860
P304
P356
10.1073/PNAS.90.17.8179
P407
P577
1993-09-01T00:00:00Z