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TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor.

Abstract：

:TDP-43, or TAR DNA-binding protein 43, is a pathological marker of a spectrum of neurodegenerative disorders, including amyotrophic lateral sclerosis and frontotemporal lobar degeneration with ubiquitin-positive inclusions. TDP-43 is an RNA/DNA-binding protein implicated in transcriptional and posttranscriptional regulation. Recent work also suggests that TDP-43 associates with cytoplasmic stress granules, which are transient structures that form in response to stress. In this study, we establish sorbitol as a novel physiological stressor that directs TDP-43 to stress granules in Hek293T cells and primary cultured glia. We quantify the association of TDP-43 with stress granules over time and show that stress granule association and size are dependent on the glycine-rich region of TDP-43, which harbors the majority of pathogenic mutations. Moreover, we establish that cells harboring wild-type and mutant TDP-43 have distinct stress responses: mutant TDP-43 forms significantly larger stress granules, and is incorporated into stress granules earlier, than wild-type TDP-43; in striking contrast, wild-type TDP-43 forms more stress granules over time, but the granule size remains relatively unchanged. We propose that mutant TDP-43 alters stress granule dynamics, which may contribute to the progression of TDP-43 proteinopathies.

journal_name

Mol Cell Biol

journal_title

Molecular and cellular biology

authors

Dewey CM,Cenik B,Sephton CF,Dries DR,Mayer P 3rd,Good SK,Johnson BA,Herz J,Yu G

doi

10.1128/MCB.01279-10

subject

Has Abstract

pub_date

2011-03-01 00:00:00

pages

1098-108

issue

5

eissn

0270-7306

issn

1098-5549

pii

MCB.01279-10

journal_volume

31

pub_type

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