Evidence map›Paper›PMID 42864327›Full record

ArticleNature communications2026

The kinase SPE-55 promotes localized assembly of the major sperm protein in Caenorhabditis elegans spermatocytes.

Nirvanjyoti Sharma Shimul, Boston T Andrew, Guinevere E Ashley, Jake P Diaz, James Matthew Ragle, Sofia De La Vega Mireles, Matthew J Wawersik, Jordan D Ward, Diane C Shakes

Abstract read
In one paragraph

Article in Nature communications, 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

9 authors.

Nirvanjyoti Sharma ShimulDepartment of Biology, William & Mary, Williamsburg, VA, USA.ORCID http://orcid.org/0009-0004-6007-8253
Boston T AndrewDepartment of Biology, William & Mary, Williamsburg, VA, USA.ORCID http://orcid.org/0009-0008-0370-3808
Guinevere E AshleyDepartment of Molecular, Cell, and Developmental Biology, University of California-Santa Cruz, Santa Cruz, CA, USA.
Jake P DiazDepartment of Biology, William & Mary, Williamsburg, VA, USA.ORCID http://orcid.org/0009-0006-2779-608X
James Matthew RagleDepartment of Molecular, Cell, and Developmental Biology, University of California-Santa Cruz, Santa Cruz, CA, USA.ORCID http://orcid.org/0000-0002-6626-2615
Sofia De La Vega MirelesDepartment of Molecular, Cell, and Developmental Biology, University of California-Santa Cruz, Santa Cruz, CA, USA.ORCID http://orcid.org/0009-0008-6206-8373
Matthew J WawersikDepartment of Biology, William & Mary, Williamsburg, VA, USA.ORCID http://orcid.org/0000-0002-3719-1926
Jordan D WardDepartment of Molecular, Cell, and Developmental Biology, University of California-Santa Cruz, Santa Cruz, CA, USA.ORCID http://orcid.org/0000-0001-9870-8936
Diane C ShakesDepartment of Biology, William & Mary, Williamsburg, VA, USA. dcshak@wm.edu.ORCID http://orcid.org/0000-0002-9677-5577

Funding

Post-translational regulation of sperm development and function in C. elegansR15GM150079 · NIGMS · COLLEGE OF WILLIAM AND MARY · PI SHAKES, DIANE CAROL · 2023 to 2023
$412k
National Science Foundation (NSF) Career Award 1942922NIGMS NIH HHS R15 GM150079U.S. Department of Health & Human Services | NIH | Office of Extramural Research, National Institutes of Health (OER) NIHR15GM150079-01
6 · The paper itself

Abstract

The crawling motility of nematode sperm is driven by the unconventional cytoskeletal protein, Major Sperm Protein (MSP). In developing spermatocytes, MSP assembles on the cytosolic side of Golgi-derived membranous organelles (MOs) in structures called Fibrous Bodies (FBs). These MSP-laden FB-MO complexes facilitate the subsequent segregation of MSP to budding spermatids and away from central residual bodies. Here we identify SPE-55 as a key FB assembly factor. In spe-55 spermatocytes, MSP remains diffusely cytosolic, and minimal MSP segregates to spermatids. The resulting spe-55 spermatozoa are motility-defective. SPE-55 localizes directly to MOs where it recruits the intrinsically disordered protein SPE-18 to initiate FB assembly, yet unlike SPE-6 or SPE-18, SPE-55 is required neither to complete meiosis nor to produce spermatids. Our study reveals an essential interplay between localized kinases and intrinsically disordered proteins in assembling large cytoskeletal complexes.

Indexed as

Caenorhabditis elegansCaenorhabditis elegans ProteinsSpermatocytesAnimalsGolgi ApparatusHelminth ProteinsMaleSpermatidsSperm MotilitySperm ProteinsCaenorhabditis elegans ProteinsHelminth Proteinsmajor sperm protein, nematodeSperm Proteins

Identifiers

PMID42864327
PMCPMC13658824

What OpenQuestion holds

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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.