Chemistry
Document Type
Article
Abstract
Ankyrin repeat (AR) domains are considered the most abundant repeat motif found in eukaryotic proteins. AR domains are predominantly known to mediate specific protein–protein interactions (PPIs) without necessarily recognizing specific primary sequences, nor requiring strict conformity within its own primary sequence. This promiscuity allows for one AR domain to recognize and bind to a variety of intracellular substrates, suggesting that AR-containing proteins may be involved in a wide array of functions. Many AR-containing proteins serve a critical role in biological processes including the ubiquitylation signaling pathway (USP). There is also strong evidence that AR-containing protein malfunction are associated with several neurological diseases and disorders. In this review, the structure and mechanism of key AR-containing proteins are discussed to suggest and/or identify how each protein utilizes their AR domains to support ubiquitylation and the cascading pathways that follow upon substrate modification.
Publication Title
International Journal of Molecular Sciences
Publication Date
1-2-2021
Volume
22
Issue
2
First Page
1
Last Page
13
ISSN
1661-6596
DOI
10.3390/ijms22020609
Keywords
Ankyrin repeat, cancer development, Deubiquitylase, E3 ubiquitin ligases, Ubiquitin, Ubiquitylation
Repository Citation
Kane, Emma I. and Spratt, Donald E., "Structural insights into ankyrin repeat-containing proteins and their influence in ubiquitylation" (2021). Chemistry. 145.
https://commons.clarku.edu/chemistry/145
Cross Post Location
Student Publications
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Copyright Conditions
Kane, E. I., & Spratt, D. E. (2021). Structural insights into ankyrin repeat-containing proteins and their influence in ubiquitylation. International journal of molecular sciences, 22(2), 609. https://doi.org/10.3390/ijms22020609
