How DNA vicinity controls SUMO E3 ligase activity

Pichler, Andrea

doi:10.15252/embj.201899705

The EMBO Journal

2018

DOI: 10.15252/embj.201899705

|View full text |Cite

How DNA vicinity controls SUMO E3 ligase activity

Andrea Pichler

Abstract: Little is known about the regulation of SUMO E3 ligases and how they are activated upon stress. New findings from the Reverter and Torres‐Rosell laboratories in The EMBO Journal demonstrate that vicinity of preferentially ssDNA activates the SUMO E3 ligase Nse2 when in complex with SMC5‐6.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2019

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

References 10 publications

(21 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

Molecular mechanisms in SUMO conjugation

Varejão

Lascorz

Liu

et al. 2019

Biochemical Society Transactions

View full text Add to dashboard Cite

The small ubiquitin-like modifier (SUMO) is a post-translational modifier that can regulate the function of hundreds of proteins inside the cell. SUMO belongs to the ubiquitin-like family of proteins that can be attached to target proteins by a dedicated enzymatic cascade pathway formed by E1, E2 and E3 enzymes. SUMOylation is involved in many cellular pathways, having in most instances essential roles for their correct function. In this review, we want to highlight the latest research on the molecular mechanisms that lead to the formation of the isopeptidic bond between the lysine substrate and the C-terminus of SUMO. In particular, we will focus on the recent discoveries on the catalytic function of the SUMO E3 ligases revealed by structural and biochemical approaches. Also, we will discuss important questions regarding specificity in SUMO conjugation, which it still remains as a major issue due to the small number of SUMO E3 ligases discovered so far, in contrast with the large number of SUMO conjugated proteins in the cell.

show abstract

Molecular mechanisms in SUMO conjugation

Varejão

Lascorz

Liu

et al. 2019

Biochemical Society Transactions

View full text Add to dashboard Cite

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

hi@scite.ai

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

How DNA vicinity controls SUMO E3 ligase activity

Cited by 1 publication

References 10 publications

Molecular mechanisms in SUMO conjugation

Molecular mechanisms in SUMO conjugation

Contact Info

Product

Resources

About