Evidence map›Paper›PMID 2326262›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1990

Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin.

A S Harris, J S Morrow

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.8field-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

32 citing papers in PubMed, 129 citations in OpenAlex.

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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 at 1 institution in 1 country.

A S HarrisDepartment of Pathology, Yale University School of Medicine, New Haven, CT 06510.
J S Morrow
Yale University · US

Funding

MEMBRANE SKELETAL CONTROL IN HEMOLYTIC DISORDERSR01HL028560 · NHLBI · YALE UNIVERSITY · PI MORROW, JON S · 1985 to 2011
$3.3M
STRUCTURE AND FUNCTION OF THE RENAL EPITHELIAL CELL MEMBRANE SKELETONP01DK038979 · NIDDK · YALE UNIVERSITY · PI MORROW, JON S · 1987 to 1998
–
STRUCTURE AND FUNCTION OF SYNAPTIC TERMINAL SPECTRINR23NS024414 · NINDS · YALE UNIVERSITY · PI HARRIS, ALAN S · 1987 to 1989
–
NHLBI NIH HHS HL28560NIDDK NIH HHS DK38979NINDS NIH HHS NS24414
6 · The paper itself

Abstract

The calcium-dependent proteolysis of fodrin has been implicated in the regulation of secretion, neutrophil and platelet activation, and long-term potentiation in neurons. In vitro studies indicate that calcium-dependent protease I (calpain I) cleaves fodrin in the middle of the alpha subunit and in the COOH-terminal third of the beta subunit. Cleavage at the beta site requires calmodulin, which binds with high affinity to a single site in the alpha subunit. In vitro binding assays, nondenaturing gel electrophoresis, and velocity sedimentation identify a linkage between calcium-dependent protease I proteolysis of fodrin and the ability of calmodulin to regulate the self-association of fodrin and its interaction with actin. Three functional states appear to exist: (i) intact fodrin, which constitutively forms tetramers and binds F-actin; (ii) alpha-cleaved fodrin, which loses its ability to self-associate and bind F-actin in the presence of calmodulin; and (iii) alpha,beta-cleaved fodrin, a form that is incompetent to establish tetramers or bind actin. Because actin binding and fodrin self-association occur at opposite ends of the molecule, whereas calmodulin binds at its center, these results indicate that long-range interactions exist within fodrin. They also offer an example of how two calcium-dependent regulatory processes may act synergistically to reversibly regulate a linkage between the membrane and the cytoskeleton.

Indexed as

ActinsAnimalsBrainCalmodulinCalpainCarrier ProteinsCattleHomeostasisMacromolecular SubstancesMicrofilament ProteinsModels, StructuralMolecular WeightNerve Tissue ProteinsProtein BindingSpectrinActinsCalmodulinCalpainCarrier ProteinsMacromolecular SubstancesMicrofilament ProteinsNerve Tissue ProteinsSpectrin

Identifiers

PMID2326262
PMCPMC53823
OpenAlexW1972982315

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.