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Boyce 4023 GlcNac Mapping Project

ABSTRACT: Bottom up proteomic analysis of gigaxonin to characterize GlcNac PTMs sites

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Erik Soderblom

LAB HEAD: Michael Boyce

PROVIDER: PXD012488 | Pride | 2019-12-12

REPOSITORIES: pride

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Dataset's files

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			Action	DRS
	ID37834.dat	Other
	ID37834.raw	Raw
	ID39968.dat	Other
	ID39968.raw	Raw

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1 - 4 of 4

Publications

Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment

Chen Po-Han PH Hu Jimin J Wu Jianli J Huynh Duc T DT Smith Timothy J TJ Pan Samuel S Bisnett Brittany J BJ Smith Alexander B AB Lu Annie A Condon Brett M BM Chi Jen-Tsan JT Boyce Michael M

JCI insight 20191126 1

Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins. Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability. Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant ...[more]

PMID: 31944090

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Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal a hierarchy of susceptibility to oxidative inactivation

Project description:Protein-S-glutathionylation (PSSG) is a post-translational modification involving the conjugation of glutathione to reactive protein thiols, which can modulate the activity and structure of key cellular proteins. Glutaredoxins (GLRX) are oxidoreductases that regulate this process by performing the reversible deglutathionylation reaction. Mammalian GLRX only requires the N-terminal cysteine in the thioredoxin domain to carry out deglutathionylation. However, GLRX has five cysteines that are potentially vulnerable to oxidative modification, and oxidation of GLRX itself has been reported in close association with aggregation and loss of activity. Further, the specific cysteines within GLRX that are vulnerable to oxidative modification and their relative reactivities with oxidants remain unknown. Herein, we utilized various molecular modeling approaches coupled with site-directed mutagenesis of each cysteine both individually and in combination to address how the five cysteines present in GLRX influence the enzyme’s biological activity and susceptibility to dimerization and inactivation. We report that mutation of cysteine 26 (C26) to serine of murine GLRX1 confers a higher rate of deglutathionylation. We further demonstrate that C8 and C83 are targets for PSSG in vitro while C79 is less vulnerable due to steric hindrance. Hydrogen peroxide also caused inactivation of GLRX that was only protected against with mutation of C8 or C83. Both experimental and modeling evidence indicates C8 contributes to dimer formation. Lastly, combinatorial mutation of C8, C26, and C83 results in increased biological activity and resistance to aggregation and oxidative inactivation. Overall, these results from our corroborated experimental and computational studies have valuable implications for the use of GLRX as a therapeutic in settings of dysregulated protein glutathionylation.

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