Evidence map›Paper›PMID 41746727›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

The Rab5 effector Rabankyrin-5 mediates endosomal fusion and trafficking of human papillomavirus during early entry.

Madison Love, Richard C Dang, Jian Xie, Pengwei Zhang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. 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
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.

  1. The endocytic fission protein EHD1 interacts with tubulin and regulates microtubule function.Biochimica et biophysica acta. Molecular cell research · 2026
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Madison LoveDepartment of Pathology, Microbiology, and Immunology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198.ORCID 0009-0003-9086-2332
Richard C DangDepartment of Genetics, Cell Biology, and Anatomy, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198.ORCID 0009-0008-9883-2206
Jian XieDepartment of Pathology, Microbiology, and Immunology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198.ORCID 0000-0003-1381-9704
Pengwei ZhangDepartment of Pathology, Microbiology, and Immunology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198.ORCID 0009-0009-5291-4238

Funding

Fundamental Training Program in Biochemistry and Molecular Biology ResearchT32GM153375 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Steven H Caplan, Ricia Katherine Hyde · 2024 to 2026
$949k
Mechanism of Dynein-mediated Early Intracellular Trafficking of Human PapillomavirusR21AI188168 · NIAID · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Pengwei Zhang · 2025 to 2026
$422k
HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) R21AI188168NIAID NIH HHS R21 AI188168NIGMS NIH HHS T32 GM153375
6 · The paper itself

Abstract

The fusion of newly formed early endosomal vesicles after endocytosis is a crucial step in viral infection. It facilitates the transition of many viruses from viral internalization to downstream intracellular trafficking within the endosomal network, ultimately enabling their delivery to intracellular replication sites. Despite its significance, the molecular mechanisms regulating the fusion of these vesicles remain poorly understood. In this study, we show that Rabankyrin-5, a Rab5 effector, is essential for the fusion of human papillomavirus (HPV)-carrying early endosomes during viral entry. Additionally, Rabankyrin-5 acts as a dynein adaptor, directly binding both the HPV minor capsid protein L2 and the dynein motor complex to link virus-carrying early endosomes to the dynein transport machinery, thereby promoting virus movement along microtubules. These dual functions enable the coordinated integration of endosomal fusion with microtubule-based transport during the early stages of viral entry.

Indexed as

EndosomesHuman Papillomavirus Virusesrab5 GTP-Binding ProteinsVirus InternalizationCapsid ProteinsDyneinsHeLa CellsHumansMicrotubulesOncogene Proteins, ViralProtein TransportCapsid ProteinsDyneinsL2 protein, Human papillomavirus type 16Oncogene Proteins, Viralrab5 GTP-Binding Proteinsdynein adaptorfusion of virus-carrying early endosomesHPV entryRabankyrin-5

Identifiers

PMID41746727
PMCPMC12956850

What OpenQuestion holds

Textmetadata
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.