Stressing the role of O-GlcNAc: linking cell survival to keratin modification.

Jeremy D Rotty, Gerald W Hart, Pierre A Coulombe
Author Information

Abstract

Mounting evidence suggests that keratin post-translational modifications are crucial for many cellular processes. Now, keratin 18 modified by the addition of an O-linked N-acetylglucosamine residue is shown to be as a critical effector of stress-responsive Akt signalling, providing an important link between keratin glycosylation and cell survival.

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MeSH Term

Acetylglucosamine
Animals
Apoptosis
Cell Survival
Chemical and Drug Induced Liver Injury
Glycosylation
Humans
Keratin-18
Keratin-8
Keratins
Models, Biological
Oximes
Phenylcarbamates
Phosphorylation
Protein Processing, Post-Translational
Proto-Oncogene Proteins c-akt
Streptozocin
beta-N-Acetylhexosaminidases
fas Receptor

Chemicals

Keratin-18
Keratin-8
Oximes
Phenylcarbamates
fas Receptor
N-acetylglucosaminono-1,5-lactone O-(phenylcarbamoyl)oxime
Streptozocin
Keratins
Akt1 protein, mouse
Proto-Oncogene Proteins c-akt
hexosaminidase C
beta-N-Acetylhexosaminidases
Acetylglucosamine

Word Cloud

Created with Highcharts 10.0.0keratincellsurvivalMountingevidencesuggestspost-translationalmodificationscrucialmanycellularprocessesNow18modifiedadditionO-linkedN-acetylglucosamineresidueshowncriticaleffectorstress-responsiveAktsignallingprovidingimportantlinkglycosylationStressingroleO-GlcNAc:linkingmodification

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