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We began analyzing https://www.nature.com/articles/nrm2293, but it redirected us to https://www.nature.com/articles/nrm2293. The analysis below is for the second page.

Title[redir]:
Concepts in sumoylation: a decade on | Nature Reviews Molecular Cell Biology
Description:
SUMO (small ubiquitin-related modifier) is a reversible post-translational protein modifier that causes molecular alterations in sumoylated target proteins, leading to changes in localization, activity and stability. In the past 10 years, mechanisms and principles that govern sumoylation have been elucidated. A decade has passed since SUMO (small ubiquitin-related modifier) was discovered to be a reversible post-translational protein modifier. During this time many enzymes that participate in regulated SUMO-conjugation and -deconjugation pathways have been identified and characterized. In parallel, the search for SUMO substrates has produced a long list of targets, which appear to be involved in most cellular functions. Sumoylation is a highly dynamic process and its outcomes are extremely diverse, ranging from changes in localization to altered activity and, in some cases, stability of the modified protein. At first glance, these effects have nothing in common; however, it seems that they all result from changes in the molecular interactions of the sumoylated proteins.

Matching Content Categories {📚}

  • Education
  • Telecommunications
  • Science

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Custom-built

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🌠 Phenomenal Traffic: 5M - 10M visitors per month


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Keywords {🔍}

pubmed, article, google, scholar, cas, sumo, biol, cell, central, protein, mol, sumoylation, nature, modification, chem, proteins, ligase, nuclear, enzyme, ubiquitin, motif, ubiquitinlike, complex, activity, ligases, transcriptional, pias, melchior, small, modifier, target, access, protease, yeast, required, transcription, sci, reversible, amino, localization, dna, ranbp, regulation, conjugation, ubc, embo, repression, function, content, information,

Topics {✒️}

permissions reprints nature portfolio privacy policy advertising article geiss-friedlander social media ubiquitin-conjugating enzyme e2–25k author information authors ran-gtpase-activating protein rangap1 development voltage-gated potassium channel sumo–rangap1–ubc9–nup358 complex covalent sumo-interaction/binding motif acetylation/deacetylation-sumoylation switch nature cell biol recognizes sumo-modified proteins covalent sumo–sim/sbm interaction telomerase-independent telomere maintenance ran gtpase-activating protein author correspondence nature rev highly sumo2/3-conjugated species small ubiquitin-related modifier nature struct consensus sumo-acceptor site c-terminal gly residue sumo-specific protease senp5 nucleolar sumo-specific proteases nature genet flexible n-terminal sequence human thymine-dna glycosylase personal data yeast hex3–slx8 heterodimer minimal sumo-binding motif human rad51/rad52 proteins sumo–e2 thioester bond ubiquitin-conjugating enzyme ubc9 ubiquitin-related protein sumo cell cycle-regulated attachment consensus acceptor sites rad6-dependent dna repair sumo-interaction/binding motif springerlink instant access daxx-dependent transcriptional repression stress-inducible sumo modification sumo-targeted ubiquitin ligases ubiquitin-dependent proteolytic control nf-κb activation permissions sentrin-activating enzyme complex

Questions {❓}

  • Does sumoylation control K2P1/TWIK1 background K+ channels?
  • PIAS proteins and transcriptional regulation — more than just SUMO E3 ligases?
  • Sumoylation in neurons: nuclear and synaptic roles?

Schema {🗺️}

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