Evidence map›Paper›PMID 21732912›Full record

ArticleThe Biochemical journal2011

MAL, but not MAL2, expression promotes the formation of cholesterol-dependent membrane domains that recruit apical proteins.

Sai P Ramnarayanan, Pamela L Tuma

Abstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Protein-enhanced small molecule disruptors of ordered membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Review
  4. Toxins · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Membrane Transport across Polarized Epithelia.Cold Spring Harbor perspectives in biology · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. 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 at 1 institution in 1 country.

Sai P RamnarayananDepartment of Biology, The Catholic University of America, NE, Washington, DC 20064, U.S.A.
Pamela L Tuma
University of America · US

Funding

MAL2 regulation of hepatic protein trafficking: mechanisms and binding partnersR01DK082890 · NIDDK · CATHOLIC UNIVERSITY OF AMERICA · PI TUMA, PAMELA L. · 2009 to 2012
$774k
MAL proteolipids in apical protein delivery in epitheliaR15GM070801 · NIGMS · CATHOLIC UNIVERSITY OF AMERICA · PI TUMA, PAMELA L · 2004 to 2004
$201k
NIDDK NIH HHS DK082890NIDDK NIH HHS R01 DK082890NIGMS NIH HHS GM070801NIGMS NIH HHS R15 GM070801
6 · The paper itself

Abstract

Our recent studies have been aimed at understanding the mechanisms regulating apical protein sorting in polarized epithelial cells. In particular, we have been investigating how lipid rafts serve to sort apical proteins in the biosynthetic pathway. The recent findings that lipid domains are too small or transient to host apically destined cargo have led to newer versions of the hypothesis that invoke proteins required for lipid domain coalescence and stabilization. MAL (myelin and lymphocyte protein) and its highly conserved family member, MAL2, have emerged as possible regulators of this process in the direct and indirect apical trafficking pathways respectively. To test this possibility, we took a biochemical approach. We determined that MAL, but not MAL2, self-associates, forms higher-order cholesterol-dependent complexes with apical proteins and promotes the formation of detergent-resistant membranes that recruit apical proteins. Such biochemical properties are consistent with a role for MAL in raft coalescence and stabilization. These findings also support a model whereby hydrophobic mismatch between the long membrane-spanning helices of MAL and the short-acyl-chain phospholipids in the Golgi drive formation of lipid domains rich in raft components that are characterized by a thicker hydrophobic core to alleviate mismatch.

Indexed as

Gene Expression RegulationVesicular Transport ProteinsAnimalsCells, CulturedCholesterolMembrane MicrodomainsMembrane ProteinsMembrane Transport ProteinsMyelin and Lymphocyte-Associated Proteolipid ProteinsMyelin ProteinsProtein Structure, TertiaryProteolipidsRatsCholesterolMAL2 protein, humanMAL protein, humanMal protein, ratMembrane ProteinsMembrane Transport ProteinsMyelin and Lymphocyte-Associated Proteolipid ProteinsMyelin ProteinsProteolipidsVesicular Transport Proteins

Identifiers

PMID21732912
PMCPMC4390122
OpenAlexW2036420840

What OpenQuestion holds

Textmetadata
LicenceTDM
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.