Expression of the 180-kD ribosome receptor induces membrane proliferation and increased secretory activity in yeast

Autor: Laura Block-Alper, Nakamura G, Becker F, Wittrup Kd, David I. Meyer, Harada J
Rok vydání: 1999
Předmět:
membrane biogenesis
Cytoplasmic and Nuclear
Receptors
Cytoplasmic and Nuclear
Golgi Apparatus
yeast
Endoplasmic Reticulum
Ribosome
Medical and Health Sciences
ribosome receptor
0302 clinical medicine
Gene Expression Regulation
Fungal
Receptors
0303 health sciences
Temperature
Biological Sciences
Cell biology
Up-Regulation
secretion
Membrane
Fungal
Original Article
Binding domain
Genes
Fungal
Saccharomyces cerevisiae
Biology
Exocytosis
Transformation
Fungal Proteins
03 medical and health sciences
Transformation
Genetic
Dogs
Aprotinin
Downregulation and upregulation
Genetic
Animals
Secretion
030304 developmental biology
Binding Sites
Endoplasmic reticulum
Cell Biology
Intracellular Membranes
Molecular biology
Peptide Fragments
Molecular Weight
Secretory protein
Gene Expression Regulation
Genes
Mutation
Ribosomes
030217 neurology & neurosurgery
Biomarkers
Developmental Biology
Zdroj: The Journal of cell biology, vol 146, iss 2
The Journal of Cell Biology
Popis: Expression of the canine 180-kD ribosome receptor (p180) in yeast cells resulted in a marked proliferation of intracellular membranes. The type of membranes observed varied with the expression of specific portions of p180. Rough membranes predominated when the ribosome binding domain of p180 was present, whereas expression constructs lacking this region resulted in smooth membranes. Northern analysis indicated that expression of the NH2-terminal 767 amino acids (ΔCT), which include the ribosome binding domain, upregulated the transcription and translation of genes involved in exocytosis. The membranes that were proliferated were functional as these cells overcame a temperature-sensitive translocation defect. Most significantly, cells that overexpressed ΔCT and proliferated rough endoplasmic reticulum exhibited severalfold higher levels of secretion of an ectopically expressed secretory protein. We conclude that p180 expression triggers a cascade of events leading to an increase in secretory potential akin to the terminal differentiation of mammalian secretory cells and tissues.
Databáze: OpenAIRE
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