Evidence map›Paper›PMID 2956266›Full record

ArticleThe Journal of cell biology1987

The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase.

K A Conzelman, M S Mooseker

Open access · bronzeAbstract read
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In one paragraph

Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

37 citing papers in PubMed, 121 citations in OpenAlex.

  1. Review
  2. Building the brush border, one microvillus at a time.Current opinion in cell biology · 2023
    Review
  3. Article
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  12. Review
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  15. Displacement-clamp measurement of the forces exerted by gating springs in the hair bundle.Proceedings of the National Academy of Sciences of the United States of America · 1993
    Article
  16. Article
  17. Article
  18. Article
  19. Purification and characterization of a mammalian myosin I.Proceedings of the National Academy of Sciences of the United States of America · 1992
    Article
  20. 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

2 authors.

K A Conzelman
M S Mooseker

Funding

STRUCTURAL ANALYSIS OF CLATHRIN-MEDIATED ENDOCYTOSISR01GM029647 · NIGMS · WASHINGTON UNIVERSITY · PI HEUSER, JOHN EDWARD · 1985 to 2008
$4.8M
NIADDK NIH HHS AM 25357NIGMS NIH HHS GM 29647
6 · The paper itself

Abstract

The microvillus 110-kD protein-calmodulin complex (designated 110K-CM) shares several properties with all myosins. In addition to its well-defined ATP-dependent binding interaction with F-actin, 110K-CM is an ATPase with diagnostically myosin-like divalent cation sensitivity. It exhibits maximum enzymatic activity in the presence of K+ and EDTA (0.24 mumol P1/mg per min) or in the presence of Ca++ (0.40 mumol P1/mg per min) and significantly less activity in physiological ionic conditions of salt and Mg++ (0.04 mumol P1/mg per min). This MgATPase is activated by F-actin in an actin concentration-dependent manner (up to 2.5-3.5-fold). The specific MgATPase activity of 110K-CM is also enhanced by the addition of 5-10 microM Ca++, but in the isolated complex, there is often also a decrease in the extent of actin activation in this range of free Ca++. Actin activation is maintained, however, in samples with exogenously added calmodulin; under these conditions, there is an approximately sevenfold stimulation of 110K-CM's enzymatic activity in the presence of 5-10 microM Ca++ and actin. 110K-CM is relatively indiscriminant in its nucleoside triphosphate specificity; in addition to ATP, GTP, CTP, UTP, and ITP are all hydrolyzed by the complex in the presence of either Mg++ or Ca++. Neither AMP nor the phosphatase substrate p-nitrophenyl phosphate are substrates for the enzymatic activity. The pH optimum for CaATPase activity is 6.0-7.5; maximum actin activation of MgATPase occurs over a broad pH range of 6.5-8.5. Finally, like myosins, purified 110K-CM crosslinks actin filaments into loosely ordered aggregates in the absence of ATP. Collectively these data support the proposal of Collins and Borysenko (1984, J. Biol. Chem., 259:14128-14135) that the 110K-CM complex is functionally analogous to the mechanoenzyme myosin.

Indexed as

Actin CytoskeletonActinsAdenosine TriphosphateAnimalsCa(2+) Mg(2+)-ATPaseCalciumCalmodulinChickensEnzyme ActivationIntestinal MucosaIntestinesMagnesiumMicrovilliPotassiumActinsAdenosine TriphosphateCa(2+) Mg(2+)-ATPaseCalciumCalmodulinMagnesiumPotassium

Identifiers

PMID2956266
PMCPMC2114910
OpenAlexW2097371819

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.