Evidence map›Paper›PMID 21762782›Full record

ReviewMolecular and cellular neurosciences2011

Mechanisms of polarized membrane trafficking in neurons -- focusing in on endosomes.

Zofia M Lasiecka, Bettina Winckler

Open access · greenAbstract readReview
In one paragraph

Review in Molecular and cellular neurosciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
4.9field-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

80 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. The Neuronal Golgi Network and Its Acolytes.Sub-cellular biochemistry · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Conserved but not critical: Trafficking and function of NaFrontiers in molecular neuroscience · 2023
    Article
  11. Article
  12. Review
  13. Dynein Is Required for Rab7-Dependent Endosome Maturation, Retrograde Dendritic Transport, and Degradation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

20 more citing papers are in PubMed but not listed here.

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.

Zofia M LasieckaDepartment of Neuroscience, University of Virginia Medical School, 409 Lane Rd. Extension, MR4-6116, Charlottesville, VA 22908, USA.
Bettina Winckler
University of Virginia · US

Funding

Targeting Pathways of Axonal Cell Adhesion MoleculesR01GM086913 · NIGMS · UNIVERSITY OF VIRGINIA · PI WINCKLER, BETTINA R · 2009 to 2012
$1.4M
NIGMS NIH HHS R01 GM086913NIGMS NIH HHS R01GM086913
6 · The paper itself

Abstract

Neurons are polarized cells that have a complex and unique morphology: long processes (axons and dendrites) extending far from the cell body. In addition, the somatodendritic and axonal domains are further divided into specific subdomains, such as synapses (pre- and postsynaptic specializations), proximal and distal dendrites, axon initial segments, nodes of Ranvier, and axon growth cones. The striking asymmetry and complexity of neuronal cells are necessary for their function in receiving, processing and transferring electrical signals, with each domain playing a precise function in these processes. In order to establish and maintain distinct neuronal domains, mechanisms must exist for protein delivery to specific neuronal compartments, such that each compartment has the correct functional molecular composition. How polarized membrane domains are established and maintained is a long-standing question. Transmembrane proteins, such as receptors and adhesion molecules, can be transported to their proper membrane domains by several pathways. The biosynthetic secretory system delivers newly synthesized transmembrane proteins from the ER via the Golgi and trans-Golgi-network (TGN) to the plasma membrane. In addition, the endosomal system is critically involved in many instances in ensuring proper (re)targeting of membrane components because it can internalize and degrade mislocalized proteins, or recycle proteins from one domain to another. The endosomal system is thus crucial for establishing and maintaining neuronal polarity. In this review, we focus mainly on the intracellular compartments that serve as sorting stations for polarized transport, with particular emphasis on the emerging roles of endosomes.

Indexed as

AnimalsCell PolarityEndosomesModels, NeurologicalNeuronsProtein Transport

Identifiers

PMID21762782
PMCPMC3205304
OpenAlexW2016394661

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.