Unknown

Dataset Information

0

Targeted in vivo O-GlcNAc sensors reveal discrete compartment-specific dynamics during signal transduction.


ABSTRACT: ?-O-N-acetyl-D-glucosamine (O-GlcNAc) is a post-translational modification involved in a plethora of biological systems ranging from cellular stress to insulin signaling. This modification shares many hallmarks with phosphorylation, including its dynamic cycling onto a host of proteins such as transcription factors, kinases, and phosphatases, and regulation of cellular functions, including cell signaling. Herein, we report the development of an improved genetically based O-GlcNAc FRET sensor and compartmentalized targeted variants for the characterization of the spatiotemporal dynamics of O-GlcNAc. During serum-stimulated signal transduction, rapid increases in O-GlcNAc activity were observed at both the plasma membrane and the nucleus, with a concomitant decrease detected in the cytoplasm. These findings suggest the existence of compartment specific dynamics for O-GlcNAc in response to signal-inducing stimuli, pointing to complex regulation of this modification. In addition, inhibition of the PI3K pathway by wortmannin abolished the O-GlcNAc response, suggesting that the activity observed is modulated downstream of the PI3K pathway. Taken together, our data argues that O-GlcNAc is a rapidly induced component of signaling and that the interplay between O-GlcNAc and kinase signaling may be more akin to the complex relationship between kinase pathways.

SUBMITTER: Carrillo LD 

PROVIDER: S-EPMC3057821 | biostudies-other | 2011 Feb

REPOSITORIES: biostudies-other

altmetric image

Publications

Targeted in vivo O-GlcNAc sensors reveal discrete compartment-specific dynamics during signal transduction.

Carrillo Luz D LD   Froemming Joshua A JA   Mahal Lara K LK  

The Journal of biological chemistry 20101207 8


β-O-N-acetyl-D-glucosamine (O-GlcNAc) is a post-translational modification involved in a plethora of biological systems ranging from cellular stress to insulin signaling. This modification shares many hallmarks with phosphorylation, including its dynamic cycling onto a host of proteins such as transcription factors, kinases, and phosphatases, and regulation of cellular functions, including cell signaling. Herein, we report the development of an improved genetically based O-GlcNAc FRET sensor and  ...[more]

Similar Datasets

| S-EPMC6908669 | biostudies-literature
| S-EPMC7327509 | biostudies-literature
| S-EPMC3266202 | biostudies-literature
| S-EPMC2788384 | biostudies-literature
| S-EPMC3789382 | biostudies-other
2022-03-03 | GSE162461 | GEO
| S-EPMC3164675 | biostudies-literature
| S-EPMC9017125 | biostudies-literature
2023-05-24 | GSE213076 | GEO
| S-EPMC5010862 | biostudies-literature