Evidence map›Paper›PMID 31661793›Full record

ArticleInternational journal of molecular sciences2019

Structural Insights into AQP2 Targeting to Multivesicular Bodies.

Jennifer Virginia Roche, Veronika Nesverova, Caroline Olsson, Peter Mt Deen, Susanna Törnroth-Horsefield

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022
    Review
  8. Article
  9. Article
  10. Review
  11. Article
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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

5 authors at 2 institutions in 2 countries.

Jennifer Virginia RocheDepartment of Biochemistry and Structural Biology, Lund University, PO Box 124, 221 00, Lund, Sweden. jennifer.roche@biochemistry.lu.se.
Veronika NesverovaDepartment of Biochemistry and Structural Biology, Lund University, PO Box 124, 221 00, Lund, Sweden. veronika.nesverova@biochemistry.lu.se.
Caroline OlssonDepartment of Biochemistry and Structural Biology, Lund University, PO Box 124, 221 00, Lund, Sweden. caroline.olsson@biochemistry.lu.se.
Peter Mt DeenDepartment of Physiology, Radboud University Medical Centre, Geert Grooteplein-Zuid 10, 6525 GA Nijmegen, The Netherlands. peterdeen11@gmail.com.
Susanna Törnroth-HorsefieldDepartment of Biochemistry and Structural Biology, Lund University, PO Box 124, 221 00, Lund, Sweden. susanna.horsefield@biochemistry.lu.se.ORCID 0000-0002-9435-8243
Lund University · SERadboud University Nijmegen · NL

Funding

Crafoordska Stiftelsen 20140811Crafoordska Stiftelsen 20180916Vetenskapsrådet 2010-5208Vetenskapsrådet 2013-05945
6 · The paper itself

Abstract

Vasopressin-dependent trafficking of AQP2 in the renal collecting duct is crucial for the regulation of water homeostasis. This process involves the targeting of AQP2 to the apical membrane during dehydration as well as its removal when hydration levels have been restored. The latter involves AQP2 endocytosis and sorting into multivesicular bodies (MVB), from where it may be recycled, degraded in lysosomes, or released into urine via exosomes. The lysosomal trafficking regulator-interacting protein 5 (LIP5) plays a crucial role in this by coordinating the actions of the endosomal sorting complex required for transport III (ESCRT-III) and vacuolar protein sorting 4 (Vps4) ATPase, resulting in the insertion of AQP2 into MVB inner vesicles. While the interaction between LIP5 and the ESCRT-III complex and Vps4 is well characterized, very little is known about how LIP5 interacts with AQP2 or any other membrane protein cargo. Here, we use a combination of fluorescence spectroscopy and computer modeling to provide a structural model of how LIP5 interacts with human AQP2. We demonstrate that, the AQP2 tetramer binds up to two LIP5 molecules and that the interaction is similar to that seen in the complex between LIP5 and the ESCRT-III component, charged multivesicular body protein 1B (CHMP1B). These studies give the very first structural insights into how LIP5 enables membrane protein insertion into MVB inner vesicles and significantly increase our understanding of the AQP2 trafficking mechanism.

Indexed as

Adenosine TriphosphatasesAquaporin 2ATPases Associated with Diverse Cellular ActivitiesEndocytosisEndosomal Sorting Complexes Required for TransportHumansMolecular Docking SimulationMultivesicular BodiesProtein MultimerizationProtein TransportSpectrometry, FluorescenceVacuolar Proton-Translocating ATPasesAdenosine TriphosphatasesAquaporin 2ATPases Associated with Diverse Cellular ActivitiesCHMP1B protein, humanEndosomal Sorting Complexes Required for TransportVacuolar Proton-Translocating ATPasesVPS4A protein, humanVTA1 protein, humanaquaporin 2lysosomal trafficking regulator-interacting protein 5multivesicular bodiesprotein sortingtraffickingwater channel

Identifiers

PMID31661793
PMCPMC6862464
OpenAlexW2981967038

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.