Evidence map›Paper›PMID 32283256›Full record

ReviewCellular signalling2020

A cut above (and below): Protein cleavage in the regulation of polycystin trafficking and signaling.

Valeria Padovano, Kavita Mistry, David Merrick, Nikolay Gresko, Michael J Caplan

Open access · greenAbstract readReview
In one paragraph

Review in Cellular signalling, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

9 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. Calcium signalling and transport in the kidney.Nature reviews. Nephrology · 2024
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
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 1 country.

Valeria PadovanoBroad Institute of MIT and Harvard, Massachusetts Institute of Technology, 415 Main Street, Cambridge, MA 02142, USA.
Kavita MistryDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026, USA.
David MerrickDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026, USA.
Nikolay GreskoDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026, USA.
Michael J CaplanDepartment of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06520-8026, USA. Electronic address: michael.caplan@yale.edu.
Yale University · USMassachusetts Institute of Technology · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007205 · NIGMS · YALE UNIVERSITY · PI KAZMIERCZAK, BARBARA I · 1985 to 2019
$42.9M
Pathways and Partners in Renal Epithelial Cell PolarityR01DK072614 · NIDDK · YALE UNIVERSITY · PI CAPLAN, MICHAEL J. · 2005 to 2022
$6.9M
In vivo Pathway Discovery in Autosomal Dominant Polycystic Kidney DiseaseRC2DK120534 · NIDDK · YALE UNIVERSITY · PI CAPLAN, MICHAEL J., SHULMAN, GERALD I · 2019 to 2023
$6.6M
NIDDK NIH HHS R01 DK072614NIDDK NIH HHS RC2 DK120534NIGMS NIH HHS T32 GM007205
6 · The paper itself

Abstract

The polycystin-1 and 2 proteins, encoded by the genes mutated in Autosomal Dominant Polycystic Kidney Disease, are connected to a large number of biological pathways. While the nature of these connections and their relevance to the primary functions of the polycystin proteins have yet to be fully elucidated, it is clear that many of them are mediated by or depend upon cleavage of the polycystin-1 protein. Cleavage of polycystin-1 at its G protein coupled receptor proteolytic site is an obligate step in the protein's maturation and in aspects of its trafficking. This cleavage may also serve to prime polycystin-1 to play a role as a non-canonical G protein coupled receptor. Cleavage of the cytoplasmic polycystin-1C terminal tail releases fragments that are able to enter the nucleus and the mitochondria and to influence their activities. Understanding the nature of these cleavages, their regulation and their consequences is likely to provide valuable insights into both the physiological functions served by the polycystin proteins and the pathological consequences of their absence.

Indexed as

Signal TransductionAnimalsCell AdhesionHumansOsteogenesisProtein TransportProteolysisTRPP Cation ChannelsTRPP Cation ChannelsCleavagePolycystinProcessingSignaling

Identifiers

PMID32283256
PMCPMC7269866
OpenAlexW3015354305

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.