Publication: UBL5/Hub1: An atypical ubiquitin-like protein with a typical role as a stress-responsive regulator
2
Issued Date
2021-09-01
Resource Type
ISSN
14220067
16616596
16616596
Other identifier(s)
2-s2.0-85113860681
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
International Journal of Molecular Sciences. Vol.22, No.17 (2021)
Suggested Citation
Sittinan Chanarat UBL5/Hub1: An atypical ubiquitin-like protein with a typical role as a stress-responsive regulator. International Journal of Molecular Sciences. Vol.22, No.17 (2021). doi:10.3390/ijms22179384 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/76052
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
UBL5/Hub1: An atypical ubiquitin-like protein with a typical role as a stress-responsive regulator
Author(s)
Other Contributor(s)
Abstract
Members of the ubiquitin-like protein family are known for their ability to modify substrates by covalent conjugation. The highly conserved ubiquitin relative UBL5/Hub1, however, is atypical because it lacks a carboxy-terminal di-glycine motif required for conjugation, and the whole E1-E2-E3 enzyme cascade is likely absent. Though the conjugation-mediated role of UBL5/Hub1 is controversial, it undoubtedly functions by interacting non-covalently with its partners. Several interactors of UBL5/Hub1 identified to date have suggested broad stress-responsive functions of the protein, for example, stress-induced control of pre-mRNA splicing, Fanconi anemia pathway of DNA damage repair, and mitochondrial unfolded protein response. While having an atypical mode of function, UBL5/Hub1 is still a stress protein that regulates feedback to various stimuli in a similar manner to other ubiquitin-like proteins. In this review, I discuss recent progress in understanding the functions of UBL5/Hub1 and the fundamental questions which remain to be answered.