Evidence map›Paper›PMID 40875111›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2025

The SUMO Pathway.

Rodrigo Martín-Rufo, Alicia Gómez-Moya, Emilio Lecona

Abstract readReview
PubMed Publisher
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Rodrigo Martín-Rufo *Centro de Biología Molecular Severo Ochoa (CBM), CSIC-UAM, Madrid, Spain.
Alicia Gómez-Moya *Centro de Biología Molecular Severo Ochoa (CBM), CSIC-UAM, Madrid, Spain.
Emilio LeconaCentro de Biología Molecular Severo Ochoa (CBM), CSIC-UAM, Madrid, Spain. elecona@cbm.csic.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin and ubiquitin-like modifiers constitute one of the most versatile systems for the control of protein function by post-translational modifications. While the ubiquitin pathway has been very well characterized, our knowledge of SUMO and its mechanisms of action is still limited. Recent technological developments have contributed to improve the basic knowledge of the biochemistry of the SUMO pathway, as well as to gain insight into the biological roles of protein SUMOylation. Here we dissect the biochemistry behind protein SUMOylation, and we describe the specific characteristics of SUMO that set it apart from the ubiquitin pathway. We cover the machinery involved in SUMO maturation, its conjugation (writers), and removal (erasers), as well as the interplay SUMO-ubiquitin. Then, we focus on the role of SUMO-interacting motifs (readers) in the recognition of protein SUMOylation, the formation of SUMO hubs, and the induction of phase separation and condensates. Last, we outline the functions of SUMO in physiology and in pathological conditions such as cancer. Our manuscript summarizes the essential knowledge about the biochemistry and regulation of the SUMO pathway.

Indexed as

Signal TransductionSmall Ubiquitin-Related Modifier ProteinsSumoylationAnimalsHumansProtein Processing, Post-TranslationalUbiquitinSmall Ubiquitin-Related Modifier ProteinsUbiquitindeSUMOylaseE1 activatingE2 conjugatingE3 ligaseSUMOSUMO-interacting motif

Identifiers

PMID40875111

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.