Evidence map›Paper›PMID 33044556›Full record

ReviewThe Journal of cell biology2020

Lysine acetylation of cytoskeletal proteins: Emergence of an actin code.

Mu A, Casey J Latario, Laura E Pickrell, Henry N Higgs

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
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

25 citing papers in PubMed, 43 citations in OpenAlex.

  1. The Many Faces of SetDB1.Epigenomes · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Tubulin post-translational modifications in meiosis.Seminars in cell & developmental biology · 2023
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. SETDB1 regulates microtubule dynamics.Cell proliferation · 2022
    Article
  19. Actin dynamics in protein homeostasis.Bioscience reports · 2022
    Review
  20. Article
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

4 authors at 1 institution in 1 country.

Mu ADepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH.
Casey J LatarioDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH.
Laura E PickrellDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH.
Henry N HiggsDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth College, Hanover, NH.
Dartmouth College · US

Funding

Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2016 to 2025
$25.9M
The impact of dynamic actin polymerization on mitochondrial dynamics and functionR35GM122545 · NIGMS · DARTMOUTH COLLEGE · PI HENRY N HIGGS · 2017 to 2026
$7.7M
INF2 in kidney function and dysfunctionR01DK088826 · NIDDK · BETH ISRAEL DEACONESS MEDICAL CENTER · PI HENRY N HIGGS, MARTIN R. POLLAK · 2010 to 2026
$6.3M
RESEARCH TRAINING IN NEPHROLOGYT32DK007199 · NIDDK · BETH ISRAEL DEACONESS MEDICAL CENTER · PI POLLAK, MARTIN R. · 1986 to 2022
$6.0M
NIDDK NIH HHS R01 DK088826NIDDK NIH HHS T32 DK007199NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R35 GM122545
6 · The paper itself

Abstract

Reversible lysine acetylation of nuclear proteins such as histones is a long-established important regulatory mechanism for chromatin remodeling and transcription. In the cytoplasm, acetylation of a number of cytoskeletal proteins, including tubulin, cortactin, and the formin mDia2, regulates both cytoskeletal assembly and stability. More recently, acetylation of actin itself was revealed to regulate cytoplasmic actin polymerization through the formin INF2, with downstream effects on ER-to-mitochondrial calcium transfer, mitochondrial fission, and vesicle transport. This finding raises the possibility that actin acetylation, along with other post-translational modifications to actin, might constitute an "actin code," similar to the "histone code" or "tubulin code," controlling functional shifts to these central cellular proteins. Given the multiple roles of actin in nuclear functions, its modifications might also have important roles in gene expression.

Indexed as

AcetylationAnimalsCytoskeletal ProteinsCytoskeletonEndoplasmic ReticulumHumansLysineMitochondriaCytoskeletal ProteinsLysine

Identifiers

PMID33044556
PMCPMC7555357
OpenAlexW3092338129

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.