5 research outputs found
Neoproterozoic to Lower Palaeozoic successions of the Tandilia System in Argentina: implication for the palaeotectonic framework of southwest Gondwana
Acthi, a thiazole biosynthesis enzyme, is essential for thiamine biosynthesis and CPC production in Acremonium chrysogenum
Late Phase of the Endoplasmic Reticulum Stress Response Pathway Is Regulated by Hog1 MAP Kinase*
When unfolded proteins accumulate in the endoplasmic reticulum (ER) causing ER stress, the unfolded protein response (UPR) responds rapidly to induce a transcriptional program that functions to alleviate the stress. However, under extreme conditions, when UPR activation is not sufficient to alleviate ER stress, the stress may persist long term. Very little is known about how the cell responds to persistent ER stress that is not resolved by the immediate activation of the UPR. We show that Hog1 MAP kinase becomes phosphorylated during the late stage of ER stress and helps the ER regain homeostasis. Although Hog1 is well known to function in osmotic stress and cell wall integrity pathways, we show that the activation mechanism for Hog1 during ER stress is distinct from both of these pathways. During late stage ER stress, upon phosphorylation, Hog1 translocates into the nucleus and regulates gene expression. Subsequently, Hog1 returns to the cytoplasm, where its phosphorylation levels remain high. From its cytoplasmic location, Hog1 contributes to the activation of autophagy by enhancing the stability of Atg8, a critical autophagy protein. Thus, Hog1 coordinates a multifaceted response to persistent ER stress
Small heat shock protein suppression of Vpr-induced cytoskeletal defects in budding yeast
Expression of the auxiliary human immunodeficiency virus type 1 (HIV-1) protein Vpr causes arrest of primate host cells in G2. Expression of this protein in budding yeast has been previously reported to cause growth arrest and a large-cell phenotype. Investigation of the effect of Vpr expression in budding yeast, reported here, showed that it causes disruption of the actin cytoskeleton. Expression of HSP42, the gene for a small heat shock protein (sHSP), from a high-copy-number plasmid reversed this effect. The sHSPs are induced by exposure of cells to thermal, osmotic, and oxidative stresses and to mitogens. In animal cells, overexpression of sHSPs causes increased resistance to stress and stabilization of actin stress fibers. Yeast cells subjected to mild stress, such as shifting from 23 to 39 degrees C, arrest growth and then resume cell division. Growth arrest is accompanied by transient disorganization of the cytoskeleton. Yeast in which the HSP42 gene was disrupted and which was subjected to moderate thermal stress reorganized the actin cytoskeleton more slowly than did wild-type control cells. These results demonstrate that in yeast, as in metazoan cells, sHSPs promote maintenance of the actin cytoskeleton