Recombinant S. cerevisiae Smt3 protein (His tag)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Smt3 also known as SUMO1 is a small ubiquitin-like modifier protein with a mass of approximately 11 kDa. It belongs to the SUMO (Small Ubiquitin-like Modifier) family and is expressed ubiquitously across many tissues. Mechanically Smt3 modifies other proteins post-translationally through a process called sumoylation. During sumoylation Smt3 covalently attaches to target proteins changing their functional properties stability subcellular localization and interactions with other proteins. This attachment typically involves lysine residues within the target protein.

Biological function summary

Smt3 influences diverse cellular processes such as nuclear transport transcriptional regulation and DNA repair. It often associates with multi-protein complexes interacting with enzymes like E1 (activating) and E2 (conjugating) involved in the SUMO pathway. Smt3 works in concert with SUMO ligases that facilitate its attachment to substrates showing that it plays a broad role in regulating cell cycle and stress responses. These functions underline the importance of Smt3 in maintaining cellular homeostasis offering insights into its versatile biological impact.

Pathways

Smt3 participates in important cellular processes such as the DNA damage response and chromatin organization pathways. Within these pathways it modulates the function of proteins such as PML (promyelocytic leukemia protein) and p53 both of which are essential for controlling cell division and maintaining genomic integrity. PML bodies heavily influenced by Smt3 serve as hubs for chromatin remodeling and gene expression regulation in response to cellular stress. Understanding Smt3's interactions within these pathways highlights its role in orchestrating a coordinated cellular response necessary for adapting to internal and external changes.

Smt3 has connections to cancer and neurodegenerative diseases. In cancers altered sumoylation patterns influenced by Smt3 impact tumor suppressors like p53 leading to deregulated cell proliferation and evasion of apoptosis. In neurodegenerative disorders aberrant sumoylation can affect proteins involved in neuronal signaling contributing to pathologies such as Huntington's disease where proteins aggregate improperly. The dynamic nature of Smt3's interactions with other proteins within these contexts suggests its potential as a therapeutic target for modulating disease progression.