Evidence map›Paper›PMID 34759380›Full record

ArticleNature structural & molecular biology2021

Scaffolding protein CcmM directs multiprotein phase separation in β-carboxysome biogenesis.

Kun Zang, Huping Wang, F Ulrich Hartl, Manajit Hayer-Hartl

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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  6. Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026
    Review
  7. Systematic determination of disulfide bond reduction potentials reveals a nonequilibrium redox hierarchy in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Architectural and biochemical advances in understanding microbial COThe Plant journal : for cell and molecular biology · 2026
    Review
  10. [COResearch square · 2026
    Article
  11. Review
  12. Article
  13. Review
  14. Structure and encapsulation of carbonic anhydrase within the α-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Engineering COPlant communications · 2025
    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.

Kun Zang *Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-7109-9154
Huping Wang *Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-9639-5355
F Ulrich HartlDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0002-7941-135X
Manajit Hayer-HartlDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany. mhartl@biochem.mpg.de.ORCID http://orcid.org/0000-0001-8213-6742
Max Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carboxysomes in cyanobacteria enclose the enzymes Rubisco and carbonic anhydrase to optimize photosynthetic carbon fixation. Understanding carboxysome assembly has implications in agricultural biotechnology. Here we analyzed the role of the scaffolding protein CcmM of the β-cyanobacterium Synechococcus elongatus PCC 7942 in sequestrating the hexadecameric Rubisco and the tetrameric carbonic anhydrase, CcaA. We find that the trimeric CcmM, consisting of γCAL oligomerization domains and linked small subunit-like (SSUL) modules, plays a central role in mediation of pre-carboxysome condensate formation through multivalent, cooperative interactions. The γCAL domains interact with the C-terminal tails of the CcaA subunits and additionally mediate a head-to-head association of CcmM trimers. Interestingly, SSUL modules, besides their known function in recruiting Rubisco, also participate in intermolecular interactions with the γCAL domains, providing further valency for network formation. Our findings reveal the mechanism by which CcmM functions as a central organizer of the pre-carboxysome multiprotein matrix, concentrating the core components Rubisco and CcaA before β-carboxysome shell formation.

Indexed as

Bacterial ProteinsBiomolecular CondensatesCarbonic AnhydrasesCryoelectron MicroscopyPhotosynthesisProtein ConformationProtein Interaction Domains and MotifsRibulose-Bisphosphate CarboxylaseSynechococcusBacterial ProteinsCarbonic AnhydrasesRibulose-Bisphosphate Carboxylase

Identifiers

PMID34759380
PMCPMC8580825
OpenAlexW3212974009

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.