Evidence map›Paper›PMID 34847774›Full record

ArticleOpen biology2021

Transmembrane topology and oligomeric nature of an astrocytic membrane protein, MLC1.

Junmo Hwang, Kunwoong Park, Ga-Young Lee, Bo Young Yoon, Hyunmin Kim, Sung Hoon Roh, Byoung-Cheol Lee, Kipom Kim, Hyun-Ho Lim

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

6 citing papers in PubMed, 9 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

9 authors at 3 institutions in 1 country.

Junmo HwangNeurovascular Unit Research Group, Korea Brain Research Institute (KBRI), 61 Cheomdan-ro, Dong-gu, Daegu 41068, Republic of Korea.
Kunwoong ParkNeurovascular Unit Research Group, Korea Brain Research Institute (KBRI), 61 Cheomdan-ro, Dong-gu, Daegu 41068, Republic of Korea.
Ga-Young LeeBrain Research Core Facility, Korea Brain Research Institute (KBRI), Daegu, Republic of Korea.
Bo Young YoonNeurovascular Unit Research Group, Korea Brain Research Institute (KBRI), 61 Cheomdan-ro, Dong-gu, Daegu 41068, Republic of Korea.
Hyunmin KimSchool of Biological Science, Institute of Molecular Biology and Genetics, Seoul National University, Seoul, Republic of Korea.
Sung Hoon RohSchool of Biological Science, Institute of Molecular Biology and Genetics, Seoul National University, Seoul, Republic of Korea.
Byoung-Cheol LeeNeurovascular Unit Research Group, Korea Brain Research Institute (KBRI), 61 Cheomdan-ro, Dong-gu, Daegu 41068, Republic of Korea.
Kipom KimBrain Research Core Facility, Korea Brain Research Institute (KBRI), Daegu, Republic of Korea.
Hyun-Ho LimNeurovascular Unit Research Group, Korea Brain Research Institute (KBRI), 61 Cheomdan-ro, Dong-gu, Daegu 41068, Republic of Korea.ORCID 0000-0002-5477-5640
Korea Brain Research Institute · KRSeoul National University · KRDaegu Gyeongbuk Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MLC1 is a membrane protein mainly expressed in astrocytes, and genetic mutations lead to the development of a leukodystrophy, megalencephalic leukoencephalopathy with subcortical cysts disease. Currently, the biochemical properties of the MLC1 protein are largely unknown. In this study, we aimed to characterize the transmembrane (TM) topology and oligomeric nature of the MLC1 protein. Systematic immunofluorescence staining data revealed that the MLC1 protein has eight TM domains and that both the N- and C-terminus face the cytoplasm. We found that MLC1 can be purified as an oligomer and could form a trimeric complex in both detergent micelles and reconstituted proteoliposomes. Additionally, a single-molecule photobleaching experiment showed that MLC1 protein complexes could consist of three MLC1 monomers in the reconstituted proteoliposomes. These results can provide a basis for both the high-resolution structural determination and functional characterization of the MLC1 protein.

Indexed as

Amino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsCytoplasmHEK293 CellsHumansMembrane ProteinsMicellesProtein DomainsProtein MultimerizationProteolipidsSingle Molecule ImagingMembrane ProteinsMicellesMLC1 protein, humanProteolipidsproteoliposomesfluorescence quenchingmembrane proteinMLC1subunit stoichiometrytransmembrane topology

Identifiers

PMID34847774
PMCPMC8633789
OpenAlexW3217218624

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Registered trials

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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.