Evidence map›Paper›PMID 17344482›Full record

ArticleMolecular biology of the cell2007

A Ser/Thr kinase required for membrane-associated assembly of the major sperm protein motility apparatus in the amoeboid sperm of Ascaris.

Kexi Yi, Shawnna M Buttery, Murray Stewart, Thomas M Roberts

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Spermatogenesis.Advances in experimental medicine and biology · 2013
    Review
  6. Review
  7. Review
  8. Nematode sperm maturation triggered by protease involves sperm-secreted serine protease inhibitor (Serpin).Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  9. Article
  10. Article
  11. Evidence for phosphorylation in the MSP cytoskeletal filaments of amoeboid spermatozoa.International journal of biochemistry and molecular biology · 2011
    Article
  12. New insights into the mechanism of fertilization in nematodes.International review of cell and molecular biology · 2011
    Review
  13. Review
  14. Article
  15. Article
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

4 authors at 2 institutions in 2 countries.

Kexi YiDepartment of Biological Science, Florida State University, Tallahassee, FL 32306, USA.
Shawnna M Buttery
Murray Stewart
Thomas M Roberts
Florida State University · USMRC Laboratory of Molecular Biology · GB

Funding

Amoeboid Motility--A Cellular and Genetic ApproachR37GM029994 · NIGMS · FLORIDA STATE UNIVERSITY · PI ROBERTS, THOMAS M · 2001 to 2010
$3.6M
AMOEBOID MOTILITY: A CELLULAR AND GENETIC APPROACHR01GM029994 · NIGMS · FLORIDA STATE UNIVERSITY · PI ROBERTS, THOMAS M · 1985 to 2000
$255k
Medical Research Council MC_U105178939NIGMS NIH HHS GM-29994NIGMS NIH HHS R01 GM029994NIGMS NIH HHS R37 GM029994
6 · The paper itself

Abstract

Leading edge protrusion in the amoeboid sperm of Ascaris suum is driven by the localized assembly of the major sperm protein (MSP) cytoskeleton in the same way that actin assembly powers protrusion in other types of crawling cell. Reconstitution of this process in vitro led to the identification of two accessory proteins required for MSP polymerization: an integral membrane phosphoprotein, MSP polymerization-organizing protein (MPOP), and a cytosolic component, MSP fiber protein 2 (MFP2). Here, we identify and characterize a 34-kDa cytosolic protein, MSP polymerization-activating kinase (MPAK) that links the activities of MPOP and MFP2. Depletion/add-back assays of sperm extracts showed that MPAK, which is a member of the casein kinase 1 family of Ser/Thr protein kinases, is required for motility. MPOP and MPAK comigrated by native gel electrophoresis, coimmunoprecipitated, and colocalized by immunofluorescence, indicating that MPOP binds to and recruits MPAK to the membrane surface. MPAK, in turn, phosphorylated MFP2 on threonine residues, resulting in incorporation of MFP2 into the cytoskeleton. Beads coated with MPAK assembled a surrounding cloud of MSP filaments when incubated in MPAK-depleted sperm extract, but only when supplemented with detergent-solubilized MPOP. Our results suggest that interactions involving MPOP, MPAK, and MFP2 focus MSP polymerization to the plasma membrane at the leading edge of the cell thereby generating protrusion and minimizing nonproductive filament formation elsewhere.

Indexed as

Amino Acid SequenceAnimalsAscaris suumIn Vitro TechniquesMaleMolecular Sequence DataPhosphorylationProtein Serine-Threonine KinasesSequence Homology, Amino AcidSpermatozoaSperm MotilityProtein Serine-Threonine Kinases

Identifiers

PMID17344482
PMCPMC1855020
OpenAlexW2113278167

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.