Evidence map›Paper›PMID 30116621›Full record

ArticleActa naturae

Role of the Scaffold Protein MIM in the Actin-Dependent Regulation of Epithelial Sodium Channels (ENaC).

L S Shuyskiy, V V Levchenko, Y A Negulyaev, A V Staruschenko, D V Ilatovskaya

Open access · hybridAbstract read
PubMed Full text at PMC
In one paragraph

Article in Acta naturae. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 53% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Cytoskeleton Rearrangements Modulate TRPC6 Channel Activity in Podocytes.International journal of molecular sciences · 2021
    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

5 authors at 3 institutions in 2 countries.

L S ShuyskiyInstitute of Cytology of RAS, Tikhoretskij Ave. 4, St. Petersburg, 194064, Russia.
V V LevchenkoDepartment of Physiology, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.
Y A NegulyaevInstitute of Cytology of RAS, Tikhoretskij Ave. 4, St. Petersburg, 194064, Russia.
A V StaruschenkoDepartment of Physiology, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.
D V IlatovskayaDepartment of Physiology, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.
Medical College of Wisconsin · USInstitute of Cytology · RUPeter the Great St. Petersburg Polytechnic University · RU

Funding

Renal ion channels in the control of blood pressureR35HL135749 · NHLBI · UNIVERSITY OF SOUTH FLORIDA · PI STARUSCHENKO, ALEXANDER · 2017 to 2023
$3.6M
Mechanisms and relevance of ENaC regulation by EGF and Rac1R01HL108880 · NHLBI · MEDICAL COLLEGE OF WISCONSIN · PI STARUSCHENKO, ALEXANDER · 2012 to 2016
$1.9M
The involvement of ATP-dependent inhibition of ENaC in ARPKD cystogenesisR00DK105160 · NIDDK · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI ILATOVSKAYA, DARIA · 2018 to 2020
$747k
The involvement of ATP-dependent inhibition of ENaC in ARPKD cystogenesisK99DK105160 · NIDDK · MEDICAL COLLEGE OF WISCONSIN · PI ILATOVSKAYA, DARIA · 2015 to 2016
$180k
NHLBI NIH HHS R01 HL108880NHLBI NIH HHS R35 HL135749NIDDK NIH HHS K99 DK105160NIDDK NIH HHS R00 DK105160
6 · The paper itself

Abstract

Epithelial Sodium Channels (ENaCs) are expressed in different organs and tissues, particularly in the cortical collecting duct (CCD) in the kidney, where they fine tune sodium reabsorption. Dynamic rearrangements of the cytoskeleton are one of the common mechanisms of ENaC activity regulation. In our previous studies, we showed that the actin-binding proteins cortactin and Arp2/3 complex are involved in the cytoskeleton-dependent regulation of ENaC and that their cooperative work decreases a channel's probability of remaining open; however, the specific mechanism of interaction between actin-binding proteins and ENaC is unclear. In this study, we propose a new component for the protein machinery involved in the regulation of ENaC, the missing-in-metastasis (MIM) protein. The MIM protein contains an IMD domain (for interaction with PIP

Indexed as

Arp2/3 complexcortactincytoskeletonENaCMIM

Identifiers

PMID30116621
PMCPMC6087825
OpenAlexW2898900489

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.