Evidence map›Paper›PMID 28663287›Full record

ArticleMolecular biology of the cell2017

CARMIL family proteins as multidomain regulators of actin-based motility.

Benjamin C Stark, M Hunter Lanier, John A Cooper

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 18% 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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
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  12. A NovelJournal of fungi (Basel, Switzerland) · 2024
    Article
  13. Article
  14. Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022
    Review
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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

3 authors at 1 institution in 1 country.

Benjamin C StarkDepartment of Biochemistry and Molecular Biophysics and Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110.
M Hunter LanierDepartment of Biochemistry and Molecular Biophysics and Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110.
John A CooperDepartment of Biochemistry and Molecular Biophysics and Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110 jacooper@wustl.edu.
Washington University in St. Louis · US

Funding

ACTIN ASSEMBLY AND CELL MOTILITY: MECHANISMS AND REGULATIONR35GM118171 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 2016 to 2020
$2.8M
REGULATION OF ACTIN CAPPING PROTEINR01GM095509 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 2012 to 2015
$1.1M
NIGMS NIH HHS R01 GM095509NIGMS NIH HHS R35 GM118171
6 · The paper itself

Abstract

CARMILs are large multidomain proteins that regulate the actin-binding activity of capping protein (CP), a major capper of actin filament barbed ends in cells. CARMILs bind directly to CP and induce a conformational change that allosterically decreases but does not abolish its actin-capping activity. The CP-binding domain of CARMIL consists of the CP-interaction (CPI) and CARMIL-specific interaction (CSI) motifs, which are arranged in tandem. Many cellular functions of CARMILs require the interaction with CP; however, a more surprising result is that the cellular function of CP in cells appears to require binding to a CARMIL or another protein with a CPI motif, suggesting that CPI-motif proteins target CP and modulate its actin-capping activity. Vertebrates have three highly conserved genes and expressed isoforms of CARMIL with distinct and overlapping localizations and functions in cells. Various domains of these CARMIL isoforms interact with plasma membranes, vimentin intermediate filaments, SH3-containing class I myosins, the dual-GEF Trio, and other adaptors and signaling molecules. These biochemical properties suggest that CARMILs play a variety of membrane-associated functions related to actin assembly and signaling. CARMIL mutations and variants have been implicated in several human diseases. We focus on roles for CARMILs in signaling in addition to their function as regulators of CP and actin.

Indexed as

Actin Capping ProteinsActin CytoskeletonActinsAmino Acid MotifsAmino Acid SequenceAnimalsCarrier ProteinsCell MembraneCell MovementHumansIntermediate FilamentsMicrofilament ProteinsModels, MolecularMyosinsProtein BindingProtein IsoformsActin Capping ProteinsActinsCARMIL1 protein, humanCarrier ProteinsMicrofilament ProteinsMyosinsProtein IsoformsVimentin

Identifiers

PMID28663287
PMCPMC5491179
OpenAlexW2731291498

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.