Evidence map›Paper›PMID 32209652›Full record

ArticleThe Journal of biological chemistry2020

The small EF-hand protein CALML4 functions as a critical myosin light chain within the intermicrovillar adhesion complex.

Myoung Soo Choi, Maura J Graves, Samaneh Matoo, Zachary A Storad, Rawnag A El Sheikh Idris, Meredith L Weck, Zachary B Smith, Matthew J Tyska, Scott W Crawley

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

29 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.The Journal of biological chemistry · 2025
    Article
  7. Article
  8. Expression, Purification, and In Vitro Analysis of Myosin.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Myoung Soo ChoiDepartment of Biological Sciences, University of Toledo, Toledo, Ohio 43606.
Maura J GravesDepartment of Biological Sciences, University of Toledo, Toledo, Ohio 43606.
Samaneh MatooDepartment of Biological Sciences, University of Toledo, Toledo, Ohio 43606.
Zachary A StoradDepartment of Biological Sciences, University of Toledo, Toledo, Ohio 43606.
Rawnag A El Sheikh IdrisDepartment of Biological Sciences, University of Toledo, Toledo, Ohio 43606.
Meredith L WeckDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37240.
Zachary B SmithDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37240.
Matthew J TyskaDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37240.
Scott W CrawleyDepartment of Biological Sciences, University of Toledo, Toledo, Ohio 43606 william.crawley@utoledo.edu.ORCID 0000-0002-4121-5353
University of Toledo · USVanderbilt University · US

Funding

Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
Molecular basis of brush border assemblyR01DK095811 · NIDDK · VANDERBILT UNIVERSITY · PI MATTHEW J TYSKA · 2013 to 2026
$4.9M
Role of I-BAR proteins in enterocyte differentiationR01DK111949 · NIDDK · VANDERBILT UNIVERSITY · PI MATTHEW J TYSKA · 2017 to 2026
$4.2M
Regulation of Brush Border Structure by Myosin-1aR01DK075555 · NIDDK · VANDERBILT UNIVERSITY · PI TYSKA, MATTHEW J · 2007 to 2016
$2.7M
Molecular basis of apical protrusion organization and function in specialized epitheliaR15GM131382 · NIGMS · UNIVERSITY OF TOLEDO · PI CRAWLEY, WILLIAM SCOTT · 2018 to 2018
$449k
Molecular basis of brush border assemblyR56DK095811 · NIDDK · VANDERBILT UNIVERSITY · PI TYSKA, MATTHEW J · 2012 to 2012
$328k
Investigating the Role of Myosin 7b in Intra-Microvillar TransportF31DK108528 · NIDDK · VANDERBILT UNIVERSITY · PI WECK, MEREDITH LYNN · 2016 to 2018
$66k
NIDDK NIH HHS F31 DK108528NIDDK NIH HHS P30 DK058404NIDDK NIH HHS R01 DK075555NIDDK NIH HHS R01 DK095811NIDDK NIH HHS R01 DK111949NIDDK NIH HHS R56 DK095811NIGMS NIH HHS R15 GM131382
6 · The paper itself

Abstract

Specialized transporting and sensory epithelial cells employ homologous protocadherin-based adhesion complexes to remodel their apical membrane protrusions into organized functional arrays. Within the intestine, the nutrient-transporting enterocytes utilize the intermicrovillar adhesion complex (IMAC) to assemble their apical microvilli into an ordered brush border. The IMAC bears remarkable homology to the Usher complex, whose disruption results in the sensory disorder type 1 Usher syndrome (USH1). However, the entire complement of proteins that comprise both the IMAC and Usher complex are not yet fully elucidated. Using a protein isolation strategy to recover the IMAC, we have identified the small EF-hand protein calmodulin-like protein 4 (CALML4) as an IMAC component. Consistent with this finding, we show that CALML4 exhibits marked enrichment at the distal tips of enterocyte microvilli, the site of IMAC function, and is a direct binding partner of the IMAC component myosin-7b. Moreover, distal tip enrichment of CALML4 is strictly dependent upon its association with myosin-7b, with CALML4 acting as a light chain for this myosin. We further show that genetic disruption of CALML4 within enterocytes results in brush border assembly defects that mirror the loss of other IMAC components and that CALML4 can also associate with the Usher complex component myosin-7a. Our study further defines the molecular composition and protein-protein interaction network of the IMAC and Usher complex and may also shed light on the etiology of the sensory disorder USH1H.

Indexed as

AnimalsCaco-2 CellsCalmodulinCell MembraneChlorocebus aethiopsCOS CellsEnterocytesHEK293 CellsHumansMiceMice, KnockoutMyosin Heavy ChainsMyosin Light ChainsMyosin Type IIUsher SyndromesCalmodulinMyh14 protein, mouseMyosin Heavy ChainsMyosin Light ChainsMyosin Type IIactinbrush bordercadherincalmodulin (CaM)calmodulin-like protein 4 (CALML4)enterocyteepithelial cellintermicrovillar adhesion complex (IMAC)intestinal epitheliumintestinemyosinprotrusionUsher syndrome

Identifiers

PMID32209652
PMCPMC7363140
OpenAlexW3013921102

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.