Deletion of yeast p24 genes activates the unfolded protein response. - Wikidata - wikimedia - TriplyDB

Deletion of yeast p24 genes activates the unfolded protein response.

Deletion of yeast p24 genes activates the unfolded protein response.

http://www.wikidata.org/entity/Q35583739

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The HAC1 gene from Pichia pastoris: characterization and effect of its overexpression on the production of secreted, surface displayed and membrane proteins Genetic analysis of yeast Yip1p function reveals a requirement for Golgi-localized rab proteins and rab-Guanine nucleotide dissociation inhibitor Molecular and cellular regulation of toll-like receptor-4 activity induced by lipopolysaccharide ligands Multicopy suppressor analysis of thermosensitive YIP1 alleles implicates GOT1 in transport from the ER Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutants.Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast.Analysis of Sec22p in endoplasmic reticulum/Golgi transport reveals cellular redundancy in SNARE protein function.Immunoisolaton of the yeast Golgi subcompartments and characterization of a novel membrane protein, Svp26, discovered in the Sed5-containing compartments.Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy.Pga1 is an essential component of Glycosylphosphatidylinositol-mannosyltransferase II of Saccharomyces cerevisiae.Sel1p/Ubx2p participates in a distinct Cdc48p-dependent endoplasmic reticulum-associated degradation pathway.Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control.A role for Yip1p in COPII vesicle biogenesis.The trafficking protein Tmed2/p24beta(1) is required for morphogenesis of the mouse embryo and placenta Disparate effects of p24alpha and p24delta on secretory protein transport and processing.Loss of p24 function in Drosophila melanogaster causes a stress response and increased levels of NF-kappaB-regulated gene products.ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate.PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis.Overexpression of an anti-CD3 immunotoxin increases expression and secretion of molecular chaperone BiP/Kar2p by Pichia pastoris ER stress-induced clearance of misfolded GPI-anchored proteins via the secretory pathway.YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins.Erv26p-dependent export of alkaline phosphatase from the ER requires lumenal domain recognition Extracellular secretion of overexpressed glycosylphosphatidylinositol-linked cell wall protein Utr2/Crh2p as a novel protein quality control mechanism in Saccharomyces cerevisiae.Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins.The Erv41p-Erv46p complex: multiple export signals are required in trans for COPII-dependent transport from the ER Role of the unfolded protein response pathway in secretory stress and regulation of INO1 expression in Saccharomyces cerevisiae.Physical protein-protein interactions predicted from microarrays The Erv41-Erv46 complex serves as a retrograde receptor to retrieve escaped ER proteins.Examination of Sec22 Homodimer Formation and Role in SNARE-dependent Membrane Fusion Transgenic neuronal overexpression reveals that stringently regulated p23 expression is critical for coordinated movement in mice Activation of the unfolded protein response pathway causes ceramide accumulation in yeast and INS-1E insulinoma cells.The COP II adaptor protein TMED7 is required to initiate and mediate the delivery of TLR4 to the plasma membrane.The endosomal protein-sorting receptor sortilin has a role in trafficking α-1 antitrypsin The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus.Dysfunction of Wntless triggers the retrograde Golgi-to-ER transport of Wingless and induces ER stress.Analysis of COPII Vesicles Indicates a Role for the Emp47-Ssp120 Complex in Transport of Cell Surface Glycoproteins.A cell-specific transgenic approach in Xenopus reveals the importance of a functional p24 system for a secretory cell.Overexpression of Sly41 suppresses COPII vesicle-tethering deficiencies by elevating intracellular calcium levels δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function.

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P2860

Deletion of yeast p24 genes activates the unfolded protein response.

http://www.wikidata.org/entity/Q35583739

description

2001 nî lūn-bûn

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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2001年论文

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2001年论文

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name

Deletion of yeast p24 genes activates the unfolded protein response.

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Deletion of yeast p24 genes activates the unfolded protein response.

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type

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Deletion of yeast p24 genes activates the unfolded protein response.

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Deletion of yeast p24 genes activates the unfolded protein response.

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prefLabel

Deletion of yeast p24 genes activates the unfolded protein response.

@ast

Deletion of yeast p24 genes activates the unfolded protein response.

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Molecular Biology of the Cell

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Deletion of yeast p24 genes activates the unfolded protein response.

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Barlowe C

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Belden WJ

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P2860

Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product

GDI1 encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway.

COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum.

Endoplasmic 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.

Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes

Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast.

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10.1091/MBC.12.4.957

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