Evidence map›Paper›PMID 38240799›Full record

ArticleThe Journal of cell biology2024

Fast-evolving cofactors regulate the role of HEATR5 complexes in intra-Golgi trafficking.

Lucas J Marmorale, Huan Jin, Thomas G Reidy, Brandon Palomino-Alonso, Christopher J Zysnarski, Fatima Jordan-Javed, Sagar Lahiri, Mara C Duncan

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of cell biology, 2024. 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, top 65% 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

1 citing paper in PubMed, 0 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Lucas J Marmorale *Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, Ann Arbor, MI, USA.ORCID 0000-0001-8926-4368
Huan Jin *Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, Ann Arbor, MI, USA.ORCID 0009-0005-4194-1311
Thomas G ReidyDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, Ann Arbor, MI, USA.ORCID 0009-0008-4340-612X
Brandon Palomino-AlonsoDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, Ann Arbor, MI, USA.ORCID 0009-0005-5125-8858
Christopher J ZysnarskiDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, Ann Arbor, MI, USA.ORCID 0000-0002-1474-9499
Fatima Jordan-JavedDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, Ann Arbor, MI, USA.ORCID 0000-0002-5939-8039
Sagar LahiriDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, Ann Arbor, MI, USA.ORCID 0000-0002-9563-6188
Mara C DuncanDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, Ann Arbor, MI, USA.ORCID 0000-0002-2383-0109
University of Michigan · US

Funding

Michigan Institute for Clinical and Health Research (MICHR)UL1TR002240 · NCATS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LUMENG, JULIE C, MASHOUR, GEORGE ALEXANDER · 2017 to 2022
$54.9M
ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
Characterizing new proteins that determine AP-1 recruitment and distributionR01GM129255 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DUNCAN, MARA C · 2019 to 2022
$1.2M
NCATS NIH HHS UL1 TR002240NIGMS NIH HHS R01 GM129255NIGMS NIH HHS R01 GM129325NIH HHS R01-GM129325
6 · The paper itself

Abstract

The highly conserved HEATR5 proteins are best known for their roles in membrane traffic mediated by the adaptor protein complex-1 (AP1). HEATR5 proteins rely on fast-evolving cofactors to bind to AP1. However, how HEATR5 proteins interact with these cofactors is unknown. Here, we report that the budding yeast HEATR5 protein, Laa1, functions in two biochemically distinct complexes. These complexes are defined by a pair of mutually exclusive Laa1-binding proteins, Laa2 and the previously uncharacterized Lft1/Yml037c. Despite limited sequence similarity, biochemical analysis and structure predictions indicate that Lft1 and Laa2 bind Laa1 via structurally similar mechanisms. Both Laa1 complexes function in intra-Golgi recycling. However, only the Laa2-Laa1 complex binds to AP1 and contributes to its localization. Finally, structure predictions indicate that human HEATR5 proteins bind to a pair of fast-evolving interacting partners via a mechanism similar to that observed in yeast. These results reveal mechanistic insight into how HEATR5 proteins bind their cofactors and indicate that Laa1 performs functions besides recruiting AP1.

Indexed as

Adaptor Proteins, Signal TransducingGolgi ApparatusSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Protein Complex 1Carrier ProteinsHumansVesicular Transport ProteinsAdaptor Protein Complex 1Adaptor Proteins, Signal TransducingCarrier ProteinsHEATR5B protein, humanLaa1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport Proteins

Identifiers

PMID38240799
PMCPMC10798858
OpenAlexW4391035162

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.