Journal article icon

Journal article

PARP1 mediated PARylation contributes to myogenic progression and glucocorticoid transcriptional response

Abstract:
The ADP-ribosyltransferase, PARP1 enzymatically generates and applies the post-translational modification, ADP-Ribose (ADPR). PARP1 roles in genome maintenance are well described, but recent work highlights roles in many fundamental processes including cellular identity and energy homeostasis. Herein, we show in both mouse and human skeletal muscle cells that PARP1-mediated PARylation is a regulator of the myogenic program and the muscle transcriptional response to steroid hormones. Chemical PARP1 modulation impacts the expression of major myocellular proteins, including troponins, key in dictating muscle contractile force. Whilst PARP1 in absence of DNA damage is often assumed to be basally inactive, we show PARylation to be acutely sensitive to extracellular glucose concentrations and the steroid hormone class, glucocorticoids which exert considerable authority over muscle tissue mass. Specifically, we find during myogenesis, a transient and significant rise in PAR. This early-stage differentiation event, if blocked with PARP1 inhibition, reduced the abundance of important muscle proteins in the fully differentiated myotubes. This suggests that PAR targets during early-stage differentiation are central to the proper development of the muscle contractile unit. We also show that reduced PARP1 in myoblasts impacts a variety of metabolic pathways in line with the recorded actions of glucocorticoids. Currently, as both regulators of myogenesis and muscle mass loss, glucocorticoids represent a clinical conundrum. Our work goes on to identify that PARP1 influences transcriptional activation by glucocorticoids of a subset of genes critical to human skeletal muscle pathology. These genes may therefore signify a regulatory battery of targets through which selective glucocorticoid modulation could be achieved. Collectively, our data provide clear links between PARP1-mediated PARylation and skeletal muscle homeostatic mechanisms crucial to tissue mass maintenance and endocrine response.
Publication status:
Published
Peer review status:
Peer reviewed

Actions

Authors

More by this author
Role:
Author
ORCID:
0000-0002-8111-803X
More by this author
Role:
Author
ORCID:
0000-0002-1127-9014
More by this author
Role:
Author
ORCID:
0000-0002-5521-7392


More from this funder
Funder identifier:
https://ror.org/003pxap67


Publisher:
Springer Nature [academic journals on nature.com]
Journal:
Cell Death Discovery More from this journal
Volume:
9
Issue:
1
Pages:
133
Article number:
133
Place of publication:
United States
Publication date:
2023-04-22
Acceptance date:
2023-03-29
DOI:
EISSN:
2058-7716
ISSN:
2058-7716
Pmid:
37087471


Language:
English
Keywords:
Pubs id:
2409676
Local pid:
pubs:2409676
Source identifiers:
W4366769160
Deposit date:
2026-04-21
ARK identifier:

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP