Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation
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 ow...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-01-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/22/2/609 |
| _version_ | 1797414003365904384 |
|---|---|
| author | Emma I. Kane Donald E. Spratt |
| author_facet | Emma I. Kane Donald E. Spratt |
| author_sort | Emma I. Kane |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-09T05:25:44Z |
| format | Article |
| id | doaj.art-deac0bc3fecb4d8eb35ef1a2c28a6f0a |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T05:25:44Z |
| publishDate | 2021-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-deac0bc3fecb4d8eb35ef1a2c28a6f0a2023-12-03T12:36:53ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-01-0122260910.3390/ijms22020609Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in UbiquitylationEmma I. Kane0Donald E. Spratt1Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main St., Worcester, MA 01610, USAGustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main St., Worcester, MA 01610, USAAnkyrin 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.https://www.mdpi.com/1422-0067/22/2/609ankyrin repeatubiquitinubiquitylationE3 ubiquitin ligasesdeubiquitylasecancer development |
| spellingShingle | Emma I. Kane Donald E. Spratt Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation International Journal of Molecular Sciences ankyrin repeat ubiquitin ubiquitylation E3 ubiquitin ligases deubiquitylase cancer development |
| title | Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation |
| title_full | Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation |
| title_fullStr | Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation |
| title_full_unstemmed | Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation |
| title_short | Structural Insights into Ankyrin Repeat-Containing Proteins and Their Influence in Ubiquitylation |
| title_sort | structural insights into ankyrin repeat containing proteins and their influence in ubiquitylation |
| topic | ankyrin repeat ubiquitin ubiquitylation E3 ubiquitin ligases deubiquitylase cancer development |
| url | https://www.mdpi.com/1422-0067/22/2/609 |
| work_keys_str_mv | AT emmaikane structuralinsightsintoankyrinrepeatcontainingproteinsandtheirinfluenceinubiquitylation AT donaldespratt structuralinsightsintoankyrinrepeatcontainingproteinsandtheirinfluenceinubiquitylation |