Evidence map›Paper›PMID 8382989›Full record

ArticleProtein science : a publication of the Protein Society1993

Mammalian integral membrane receptors are homologous to facilitators and antiporters of yeast, fungi, and eubacteria.

J Reizer, K Finley, D Kakuda, C L MacLeod, A Reizer, M H Saier

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Protein science : a publication of the Protein Society, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 90 citations in OpenAlex.

  1. Control of asparagine homeostasis inJournal of bacteriology · 2024
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  19. Proton-dependent multidrug efflux systems.Microbiological reviews · 1996
    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

6 authors at 2 institutions in 1 country.

J ReizerDepartment of Biology, University of California, San Diego, La Jolla 92093.
K Finley
D Kakuda
C L MacLeod
A Reizer
M H Saier
University of California, San Diego · USCancer Genetics (United States) · US

Funding

MECHANISM OF CARBOHYDRATE TRANSPORT IN BACTERIAR01AI014176 · NIAID · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI SAIER, MILTON H. · 1986 to 2000
$294k
ATP-DEPENDENT PROTEIN KINASES IN STREPTOCOCCIR01AI021702 · NIAID · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI SAIER, MILTON H. · 1985 to 1996
–
NIAID NIH HHS 2RO1AI14176NIAID NIH HHS 5RO1AI21702PHS HHS 8RO137778
6 · The paper itself

Abstract

We demonstrate that three integral membrane receptors of mammals--the ecotropic retroviral leukemia receptor (ERR), the human retroviral receptor (HRR), and the T-cell early activator (Tea)--are homologous to a family of transporters specific for amino acids, polyamines, and choline (APC), which catalyze solute uniport, solute:cation symport, or solute:solute antiport in yeast, fungi, and eubacteria. Interestingly, the ERR membrane protein was recently shown to function as a cation:amino acid cotransporter. A binary sequence similarity matrix and an evolutionary tree of the 14 members of this family, illustrating their sequence similarities and divergences, were constructed. Other proteins, including the developmentally controlled GerAII spore germination protein of Bacillus subtilis and the acetylcholine receptor of Drosophila melanogaster gave sequence comparison scores of a sufficiently large magnitude to suggest (but not to establish) a common evolutionary origin with members of the APC family. We report an extended and corrected Tea cDNA sequence and show that the mammalian Tea and ERR encoding genes are differentially expressed in tissues and cell lines. Furthermore, the two mammalian cDNA sequences hybridize with other vertebrate and yeast genomic DNAs under stringent conditions. These observations support the notion that cell surface receptor proteins in mammals are transport proteins that share a common origin with transport proteins of single-celled organisms. Thus, permeases of essential metabolites may function pathologically as viral receptors.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsBase SequenceCarrier ProteinsDNAFungal ProteinsHumansMembrane ProteinsMolecular Sequence DataPhylogenyReceptors, Cell SurfaceSequence Homology, Amino AcidSpecies SpecificityBacterial ProteinsCarrier ProteinsDNAFungal ProteinsMembrane ProteinsReceptors, Cell Surface

Identifiers

PMID8382989
PMCPMC2142299
OpenAlexW2097600251

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.