Evidence map›Paper›PMID 10880570›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

The central cytoplasmic loop of the major facilitator superfamily of transport proteins governs efficient membrane insertion.

A B Weinglass, H R Kaback

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Key computational findings reveal proton transfer as driving the functional cycle in the phosphate transporter PiPT.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. Article
  5. Efflux pump proteins in antifungal resistance.Frontiers in pharmacology · 2014
    Review
  6. Article
  7. Article
  8. Structural basis of GLUT1 inhibition by cytoplasmic ATP.The Journal of general physiology · 2007
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Engineering a terbium-binding site into an integral membrane protein for luminescence energy transfer.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  17. Article
  18. 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

2 authors.

A B WeinglassHoward Hughes Medical Institute, Departments of Physiology and Microbiology and Molecular Genetics, Molecular Biology Institute, University of California, Los Angeles, CA 90095-1662, USA.
H R Kaback

Funding

NEW APPROACHES TO MEMBRANE PROTEIN STRUCTURESR01DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 1996 to 2014
$5.2M
Dynamics of the Lactose Permease of Escherichia ColiR56DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2015 to 2015
$154k
NIDDK NIH HHS DK51131NIDDK NIH HHS R01 DK051131NIDDK NIH HHS R56 DK051131
6 · The paper itself

Abstract

Deletion of 5 residues (Delta5) from the central cytoplasmic loop of the lactose permease of Escherichia coli has no significant effect on expression or activity, whereas Delta12 leads to increased rates of permease turnover after membrane insertion and decreased transport activity, and Delta20 abolishes insertion and activity. By expressing Delta12 or Delta20 in two halves, both expression and activity are restored to levels approximating wild type. Replacing deleted residues with random hydrophilic amino acids also leads to full recovery. However, introduction of hydrophobic residues decreases expression and activity in a context-dependent manner. Thus, a minimum length of the central cytoplasmic loop is vital for proper insertion, stability, and efficient transport activity, because of constraints at the cytoplasmic ends of helices VI and VII. Furthermore, the results are consistent with the idea that the middle cytoplasmic loop provides a temporal delay between insertion of the first six helices into the membrane before insertion of the second six helices.

Indexed as

Escherichia coli ProteinsMonosaccharide Transport ProteinsSymportersAmino Acid SequenceBiological TransportCell MembraneCytoplasmEscherichia coliHydrolysisMembrane Transport ProteinsMolecular Sequence DataMutagenesis, Site-DirectedSequence DeletionSequence Homology, Amino AcidEscherichia coli Proteinslactose permeaseLacY protein, E coliMembrane Transport ProteinsMonosaccharide Transport ProteinsSymporters

Identifiers

PMID10880570
PMCPMC16800

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.