Loss of p24 function in Drosophila melanogaster causes a stress response and increased levels of NF-kappaB-regulated gene products.

ABSTRACT:

Background

Secretory and transmembrane proteins traverse the endoplasmic reticulum (ER) and Golgi compartments for final maturation prior to reaching their functional destinations. Members of the p24 protein family, which are transmembrane constituents of ER and Golgi-derived transport vesicles, function in trafficking some secretory proteins in yeast and higher eukaryotes. Yeast p24 mutants have minor secretory defects and induce an ER stress response that likely results from accumulation of proteins in the ER due to disrupted trafficking. We tested the hypothesis that loss of Drosophila melanogaster p24 protein function causes a transcriptional response characteristic of ER stress activation.

Results

We performed genome-wide profiling experiments on tissues from Drosophila

SUBMITTER: Boltz KA 

PROVIDER: S-EPMC2396179 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature