Menu
×
John L. Dart Library
Closed
Phone: (843) 722-7550
West Ashley Library
Closed
Phone: (843) 766-6635
Folly Beach Library
Closed
Phone: (843) 588-2001
Edgar Allan Poe/Sullivan's Island Library
Closed for renovations
Phone: (843) 883-3914
Wando Mount Pleasant Library
Closed
Phone: (843) 805-6888
Village Library
Closed
Phone: (843) 884-9741
St. Paul's/Hollywood Library
Closed
Phone: (843) 889-3300
Otranto Road Library
Closed
Phone: (843) 572-4094
Mt. Pleasant Library
Closed
Phone: (843) 849-6161
McClellanville Library
Closed
Phone: (843) 887-3699
Keith Summey North Charleston Library
Closed
Phone: (843) 744-2489
John's Island Library
Closed
Phone: (843) 559-1945
Hurd/St. Andrews Library
Closed
Phone: (843) 766-2546
Miss Jane's Building (Edisto Library Temporary Location)
Closed
Phone: (843) 869-2355
Dorchester Road Library
Closed
Phone: (843) 552-6466
Baxter-Patrick James Island
Closed
Phone: (843) 795-6679
Main Library
2 p.m. – 5 p.m.
Phone: (843) 805-6930
Bees Ferry West Ashley Library
Closed
Phone: (843) 805-6892
Mobile Library
Closed
Phone: (843) 805-6909
Today's Hours
John L. Dart Library
Closed
Phone: (843) 722-7550
West Ashley Library
Closed
Phone: (843) 766-6635
Folly Beach Library
Closed
Phone: (843) 588-2001
Edgar Allan Poe/Sullivan's Island Library
Closed for renovations
Phone: (843) 883-3914
Wando Mount Pleasant Library
Closed
Phone: (843) 805-6888
Village Library
Closed
Phone: (843) 884-9741
St. Paul's/Hollywood Library
Closed
Phone: (843) 889-3300
Otranto Road Library
Closed
Phone: (843) 572-4094
Mt. Pleasant Library
Closed
Phone: (843) 849-6161
McClellanville Library
Closed
Phone: (843) 887-3699
Keith Summey North Charleston Library
Closed
Phone: (843) 744-2489
John's Island Library
Closed
Phone: (843) 559-1945
Hurd/St. Andrews Library
Closed
Phone: (843) 766-2546
Miss Jane's Building (Edisto Library Temporary Location)
Closed
Phone: (843) 869-2355
Dorchester Road Library
Closed
Phone: (843) 552-6466
Baxter-Patrick James Island
Closed
Phone: (843) 795-6679
Main Library
2 p.m. – 5 p.m.
Phone: (843) 805-6930
Bees Ferry West Ashley Library
Closed
Phone: (843) 805-6892
Mobile Library
Closed
Phone: (843) 805-6909
Patron Login
menu
Item request has been placed!
×
Item request cannot be made.
×
Processing Request
A critical discussion on the relationship between E3 ubiquitin ligases, protein degradation, and skeletal muscle wasting: it's not that simple.
Item request has been placed!
×
Item request cannot be made.
×
Processing Request
- Author(s): Hughes, David C.; Goodman, Craig A.; Baehr, Leslie M.; Gregorevic, Paul; Bodine, Sue C.
- Source:
American Journal of Physiology: Cell Physiology; Dec2023, Vol. 325 Issue 6, pC1567-C1582, 16p- Subject Terms:
- Source:
- Additional Information
- Abstract: Ubiquitination is an important post-translational modification (PTM) for protein substrates, whereby ubiquitin is added to proteins through the coordinated activity of activating (E1), ubiquitin-conjugating (E2), and ubiquitin ligase (E3) enzymes. The E3s provide key functions in the recognition of specific protein substrates to be ubiquitinated and aid in determining their proteolytic or nonproteolytic fates, which has led to their study as indicators of altered cellular processes. MuRF1 and MAFbx/Atrogin-1 were two of the first E3 ubiquitin ligases identified as being upregulated in a range of different skeletal muscle atrophy models. Since their discovery, the expression of these E3 ubiquitin ligases has often been studied as a surrogate measure of changes to bulk protein degradation rates. However, emerging evidence has highlighted the dynamic and complex regulation of the ubiquitin proteasome system (UPS) in skeletal muscle and demonstrated that protein ubiquitination is not necessarily equivalent to protein degradation. These observations highlight the potential challenges of quantifying E3 ubiquitin ligases as markers of protein degradation rates or ubiquitin proteasome system (UPS) activation. This perspective examines the usefulness of monitoring E3 ubiquitin ligases for determining specific or bulk protein degradation rates in the settings of skeletal muscle atrophy. Specific questions that remain unanswered within the skeletal muscle atrophy field are also identified, to encourage the pursuit of new research that will be critical in moving forward our understanding of the molecular mechanisms that govern protein function and degradation in muscle. [ABSTRACT FROM AUTHOR]
- Abstract: Copyright of American Journal of Physiology: Cell Physiology is the property of American Physiological Society and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
- Abstract:
Contact CCPL
Copyright 2022 Charleston County Public Library Powered By EBSCO Stacks 3.3.0 [350.3] | Staff Login
No Comments.