Evidence map›Paper›PMID 22779703›Full record

ArticleMolecular microbiology2012

Modulation of Leishmania major aquaglyceroporin activity by a mitogen-activated protein kinase.

Goutam Mandal, Mansi Sharma, Martin Kruse, Claudia Sander-Juelch, Laura A Munro, Yong Wang, Jenny Veide Vilg, Markus J Tamás, Hiranmoy Bhattacharjee, Martin Wiese and 1 more

Abstract read
In one paragraph

Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

30 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Non-Vesicular Lipid Transport Machinery inInternational journal of molecular sciences · 2023
    Review
  3. Review
  4. Promastigote-to-Amastigote Conversion inPathogens (Basel, Switzerland) · 2022
    Review
  5. Article
  6. Article
  7. Review
  8. Microorganisms · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Molecular Analysis ofJournal of arthropod-borne diseases · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Functional role of lysine 12 in Leishmania major AQP1.Molecular and biochemical parasitology · 2015
    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

11 authors at 6 institutions in 5 countries.

Goutam MandalDepartment of Molecular Microbiology and Infectious Diseases, Florida International University, Herbert Wertheim College of Medicine, Miami, FL, USA.
Mansi Sharma
Martin Kruse
Claudia Sander-Juelch
Laura A Munro
Yong Wang
Jenny Veide Vilg
Markus J Tamás
Hiranmoy Bhattacharjee
Martin Wiese
Rita Mukhopadhyay
Bernhard Nocht Institute for Tropical Medicine · DEUniversity of Gothenburg · SEUniversity of Strathclyde · GBIn-Q-Tel · USUniversity of Turku · FIWayne State University · US

Funding

Mechanisms of arsenical transportR37GM055425 · NIGMS · WAYNE STATE UNIVERSITY · PI ROSEN, BARRY P. · 2005 to 2014
$4.4M
Mechanisms of Arsenic Transport and BiotransformationsR01GM055425 · NIGMS · WAYNE STATE UNIVERSITY · PI ROSEN, BARRY P. · 1997 to 2019
$3.8M
Metalloid transporters and drug resistance in LeishmaniaR01AI058170 · NIAID · WAYNE STATE UNIVERSITY · PI MUKHOPADHYAY, RITA · 2005 to 2009
$978k
NIAID NIH HHS AI58170NIAID NIH HHS R01 AI058170NIGMS NIH HHS GM55425NIGMS NIH HHS R01 GM055425NIGMS NIH HHS R37 GM055425
6 · The paper itself

Abstract

Leishmania major aquaglyceroporin (LmjAQP1) adventitiously facilitates the uptake of antimonite [Sb(III)], an active form of Pentostam® or Glucantime®, which are the first line of defence against all forms of leishmaniasis. The present paper shows that LmjAQP1 activity is modulated by the mitogen-activated protein kinase, LmjMPK2. Leishmania parasites coexpressing LmjAQP1 and LmjMPK2 show increased Sb(III) uptake and increased Sb(III) sensitivity. When subjected to a hypo-osmotic stress, these cells show faster volume recovery than cells expressing LmjAQP1 alone. LmjAQP1 is phosphorylated in vivo at Thr-197 and this phosphorylation requires LmjMPK2 activity. Lys-42 of LmjMPK2 is critical for its kinase activity. Cells expressing altered T197A LmjAQP1 or K42A LmjMPK2 showed decreased Sb(III) influx and a slower volume recovery than cells expressing wild-type proteins. Phosphorylation of LmjAQP1 led to a decrease in its turnover rate affecting LmjAQP1 activity. Although LmjAQP1 is localized to the flagellum of promastigotes, upon phosphorylation, it is relocalized to the entire surface of the parasite. Leishmania mexicana promastigotes with an MPK2 deletion showed reduced Sb(III) uptake and slower volume recovery than wild-type cells. This is the first report where a parasite aquaglyceroporin activity is post-translationally modulated by a mitogen-activated protein kinase.

Indexed as

AntimonyAntiprotozoal AgentsAquaporin 1Gene DeletionLeishmania majorLeishmania mexicanaMitogen-Activated Protein KinasesParasitic Sensitivity TestsantimoniteAntimonyAntiprotozoal AgentsAquaporin 1Mitogen-Activated Protein Kinases

Identifiers

PMID22779703
PMCPMC3438341
OpenAlexW1486471936

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.