HOG1 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.
Johnston M, Hillier L, Riles L, Albermann K, Andr? B, Ansorge W, Benes V, Br?ckner M, Delius H, Dubois E, D?sterh?ft A, Entian KD, Floeth M, Goffeau A, Hebling U, Heumann K, Heuss-Neitzel D, Hilbert H, Hilger F, Kleine K, K?tter P, Louis EJ, Messenguy F, Mewes HW, Hoheisel JD
Nature387(6632 Suppl)87-90(1997 May)

Life with 6000 genes.
Goffeau A, Barrell BG, Bussey H, Davis RW, Dujon B, Feldmann H, Galibert F, Hoheisel JD, Jacq C, Johnston M, Louis EJ, Mewes HW, Murakami Y, Philippsen P, Tettelin H, Oliver SG
Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

Hog1 phosphorylates the Spt4 elongation factor at Thr42 and Ser43 and such phosphorylations are essential for the overall transcriptional response upon osmostress.
Title: Regulation of transcription elongation in response to osmostress.

Data suggest that Rck2 appears to act as a central hub for many Hog1-mediated secondary phosphorylation events.
Title: Identifying protein kinase-specific effectors of the osmostress response in yeast.

Studied osmotic stress tolerance in Saccharomyces cerevisiae; found OLE1 overexpression improves stress tolerance and activates Hog1 pathway.
Title: Overexpression of OLE1 enhances stress tolerance and constitutively activates the MAPK HOG pathway in Saccharomyces cerevisiae.

Proteomic and metabolomic comparisons revealed that the xylose-metabolizing mutant strains exhibit altered metabolic pathways relative to the parental strain when grown in xylose. Further analyses revealed that interacting mutations in HOG1 and ISU1 unexpectedly elevated mitochondrial respiratory proteins and enabled rapid aerobic respiration of xylose and other non-fermentable carbon substrates.
Title: Directed Evolution Reveals Unexpected Epistatic Interactions That Alter Metabolic Regulation and Enable Anaerobic Xylose Use by Saccharomyces cerevisiae.

Report shows that Slt2 is phosphorylated following arsenite treatment. Slt2 and its kinase activity are necessary for full acquisition of arsenite tolerance and this effect appears to be mediated through Fps1. Hence, it appears that two MAPKs, Hog1 and Slt2, collaborate in controlling arsenite influx and efflux through Fps1 suggesting a mechanism where this MAPK collaboration may function on Fps1.
Title: The mitogen-activated protein kinase Slt2 modulates arsenite transport through the aquaglyceroporin Fps1.