Evidence map›Paper›PMID 22875993›Full record

ArticleMolecular biology of the cell2012

Alternative splicing results in RET isoforms with distinct trafficking properties.

Douglas S Richardson, David M Rodrigues, Brandy D Hyndman, Mathieu J F Crupi, Adrian C Nicolescu, Lois M Mulligan

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

40 citing papers in PubMed, 67 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Douglas S RichardsonDepartment of Pathology and Molecular Medicine and Division of Cancer Biology and Genetics, Cancer Research Institute, Queen's University, Kingston, ON, Canada.
David M Rodrigues
Brandy D Hyndman
Mathieu J F Crupi
Adrian C Nicolescu
Lois M Mulligan
Queen's University · CA

Funding

Canadian Institutes of Health Research MOP49602
6 · The paper itself

Abstract

RET encodes a receptor tyrosine kinase that is essential for spermatogenesis, development of the sensory, sympathetic, parasympathetic, and enteric nervous systems and the kidneys, as well as for maintenance of adult midbrain dopaminergic neurons. RET is alternatively spliced to encode multiple isoforms that differ in their C-terminal amino acids. The RET9 and RET51 isoforms display unique levels of autophosphorylation and have differential interactions with adaptor proteins. They induce distinct gene expression patterns, promote different levels of cell differentiation and transformation, and play unique roles in development. Here we present a comprehensive study of the subcellular localization and trafficking of RET isoforms. We show that immature RET9 accumulates intracellularly in the Golgi, whereas RET51 is efficiently matured and present in relatively higher amounts on the plasma membrane. RET51 is internalized faster after ligand binding and undergoes recycling back to the plasma membrane. This differential trafficking of RET isoforms produces a more rapid and longer duration of signaling through the extracellular-signal regulated kinase/mitogen-activated protein kinase pathway downstream of RET51 relative to RET9. Together these differences in trafficking properties contribute to some of the functional differences previously observed between RET9 and RET51 and establish the important role of intracellular trafficking in modulating and maintaining RET signaling.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsCell LineCell MembraneCell NucleusCoculture TechniquesEndosomesGlial Cell Line-Derived Neurotrophic FactorGolgi ApparatusHumansLysosomesMAP Kinase Signaling SystemMolecular Sequence DataProtein IsoformsProtein Processing, Post-TranslationalGlial Cell Line-Derived Neurotrophic FactorProtein IsoformsProto-Oncogene Proteins c-retrab11 GTP-Binding Proteinsrab GTP-Binding ProteinsRET protein, human

Identifiers

PMID22875993
PMCPMC3459860
OpenAlexW2160482646

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.