Evidence map›Paper›PMID 42244606›Full record

ArticlebioRxiv : the preprint server for biology2026

Activating adaptor-like sequences in pericentrin mediate its transport by dynein.

Wenzhu Zhang, Ami G Sangster, Thao T Nguyen, Samantha Melancon, Jia-Lin Shiu, Tian Hao Huang, Akhil G Iragavarapu, Xueer Jiang, Jennielee Mia, Halil Aydin and 2 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Wenzhu ZhangDepartment of Biology, Syracuse University, Syracuse, New York, USA.
Ami G SangsterDepartment of Cell & Systems Biology, University of Toronto, Toronto, Ontario, Canada.
Thao T NguyenDepartment of Biology, Syracuse University, Syracuse, New York, USA.
Samantha MelanconDepartment of Biology, Syracuse University, Syracuse, New York, USA.
Jia-Lin ShiuDepartment of Biology, Syracuse University, Syracuse, New York, USA.
Tian Hao HuangDepartment of Cell & Systems Biology, University of Toronto, Toronto, Ontario, Canada.
Akhil G IragavarapuDepartment of Molecular Pathobiology, New York University, New York, New York, USA.
Xueer JiangDepartment of Cell Biology and Human Anatomy, University of California, Davis, School of Medicine, Davis, California, USA.
Jennielee MiaDepartment of Cell Biology and Human Anatomy, University of California, Davis, School of Medicine, Davis, California, USA.
Halil AydinDepartment of Molecular Pathobiology, New York University, New York, New York, USA.ORCID 0000-0002-5409-3797
Alan M MosesDepartment of Cell & Systems Biology, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0001-7099-8257
Li-En JaoDepartment of Biology, Syracuse University, Syracuse, New York, USA.ORCID 0000-0001-5925-883X

Funding

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
Mechanism of centrosome maturation in vertebratesR01GM144435 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI Li-En Jao · 2022 to 2026
$1.7M
NIGMS NIH HHS R01 GM129325NIGMS NIH HHS R01 GM144435
6 · The paper itself

Abstract

Right before a cell divides, the centrosome rapidly increases its size and microtubule organizing activity through a process termed centrosome maturation. PCNT, a coiled-coil centrosomal protein, is synthesized and transported to the centrosome simultaneously by dynein. This dynein-mediated co-translational transport of PCNT facilitates centrosome maturation and mitotic spindle formation. How dynein engages and transports PCNT, however, remains unclear. Here we find that PCNT residues 1393-1525 are required for mediating dynein-dynactin interaction. PCNT (1393-1525) also shares similar sequence features with canonical dynein cargo adaptors. PCNT is predicted to interact with dynein heavy chains through similar contact sites used by canonical dynein cargo adaptors. Introducing point mutations at those contact sites abolishes dynein-mediated transport in a peroxisome motility assay. Our results suggest that PCNT contains adaptor-like sequences to bind and activate dynein directly during its transport to the centrosome. Our data also suggest that dynein may engage with some of its cargoes directly without an adaptor.

Indexed as

AlphaFoldcentrosomecoiled coilsco-translational transportdyneinPericentrinpericentriolar material

Identifiers

PMID42244606
PMCPMC13232285

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.