Evidence map›Paper›PMID 38472649›Full record

ArticleNature neuroscience2024

Liprin-α proteins are master regulators of human presynapse assembly.

Berta Marcó de la Cruz, Joaquín Campos, Angela Molinaro, Xingqiao Xie, Gaowei Jin, Zhiyi Wei, Claudio Acuna, Fredrik H Sterky

Open access · hybridAbstract read
In one paragraph

Article in Nature neuroscience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

24 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Liprin-α family proteins and their cellular functions.The Journal of biological chemistry · 2026
    Review
  4. Article
  5. Munc13 serves as a molecular filter for SNARE sorting and assembly in active zone condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Liquid-liquid phase separation in neural development.Cellular and molecular life sciences : CMLS · 2026
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Biogenesis and reformation of synaptic vesicles.The Journal of physiology · 2025
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 5 institutions in 3 countries.

Berta Marcó de la Cruz *Department of Laboratory Medicine, Institute for Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.ORCID http://orcid.org/0009-0003-5209-6577
Joaquín Campos *Chica and Heinz Schaller Foundation, Institute of Anatomy and Cell Biology, Heidelberg University, Heidelberg, Germany.
Angela MolinaroDepartment of Laboratory Medicine, Institute for Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Xingqiao XieSchool of Life Sciences, Southern University of Science and Technology, Shenzhen, China.
Gaowei JinSchool of Life Sciences, Southern University of Science and Technology, Shenzhen, China.
Zhiyi WeiSchool of Life Sciences, Southern University of Science and Technology, Shenzhen, China.ORCID http://orcid.org/0000-0002-4446-6502
Claudio AcunaChica and Heinz Schaller Foundation, Institute of Anatomy and Cell Biology, Heidelberg University, Heidelberg, Germany. acuna@uni-heidelberg.de.ORCID http://orcid.org/0000-0002-8849-6260
Fredrik H SterkyDepartment of Laboratory Medicine, Institute for Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden. fredrik.sterky@gu.se.ORCID http://orcid.org/0000-0001-8881-0523
Heidelberg University · DEShenzhen University · CNUniversity of Gothenburg · SESahlgrenska University Hospital · SESouthern University of Science and Technology · CN

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) SFB1158-SO2Fritz Thyssen Stiftung (Fritz Thyssen Foundation) 10.21.0.019MNJeanssons Stiftelser (Jeansson Foundations) JS2016-0026Vetenskapsrådet (Swedish Research Council) 2016-00968Vetenskapsrådet (Swedish Research Council) 2017-03331
6 · The paper itself

Abstract

The formation of mammalian synapses entails the precise alignment of presynaptic release sites with postsynaptic receptors but how nascent cell-cell contacts translate into assembly of presynaptic specializations remains unclear. Guided by pioneering work in invertebrates, we hypothesized that in mammalian synapses, liprin-α proteins directly link trans-synaptic initial contacts to downstream steps. Here we show that, in human neurons lacking all four liprin-α isoforms, nascent synaptic contacts are formed but recruitment of active zone components and accumulation of synaptic vesicles is blocked, resulting in 'empty' boutons and loss of synaptic transmission. Interactions with presynaptic cell adhesion molecules of either the LAR-RPTP family or neurexins via CASK are required to localize liprin-α to nascent synaptic sites. Liprin-α subsequently recruits presynaptic components via a direct interaction with ELKS proteins. Thus, assembly of human presynaptic terminals is governed by a hierarchical sequence of events in which the recruitment of liprin-α proteins by presynaptic cell adhesion molecules is a critical initial step.

Indexed as

SynapsesSynaptic TransmissionAnimalsCarrier ProteinsCell Adhesion MoleculesHumansMammalsNeuronsPresynaptic TerminalsCarrier ProteinsCell Adhesion Molecules

Identifiers

PMID38472649
PMCPMC11001580
OpenAlexW4392705750

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.