Evidence map›Paper›PMID 34172739›Full record

ArticleNature communications2021

The nanoscale molecular morphology of docked exocytic dense-core vesicles in neuroendocrine cells.

Bijeta Prasai, Gideon J Haber, Marie-Paule Strub, Regina Ahn, John A Ciemniecki, Kem A Sochacki, Justin W Taraska

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 22 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

7 authors at 1 institution in 1 country.

Bijeta PrasaiBiochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.ORCID 0000-0002-7824-6954
Gideon J HaberBiochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.ORCID 0000-0002-5034-6355
Marie-Paule StrubBiochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Regina AhnBiochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
John A CiemnieckiBiochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Kem A SochackiBiochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Justin W TaraskaBiochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA. justin.taraska@nih.gov.ORCID 0000-0001-5355-9535
National Institutes of Health · US

Funding

Architecture and control of vesicle fusion in excitable cellsZIAHL006098 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI TARASKA, JUSTIN · 2011 to 2025
$25.5M
Intramural NIH HHS ZIA HL006098
6 · The paper itself

Abstract

Rab-GTPases and their interacting partners are key regulators of secretory vesicle trafficking, docking, and fusion to the plasma membrane in neurons and neuroendocrine cells. Where and how these proteins are positioned and organized with respect to the vesicle and plasma membrane are unknown. Here, we use correlative super-resolution light and platinum replica electron microscopy to map Rab-GTPases (Rab27a and Rab3a) and their effectors (Granuphilin-a, Rabphilin3a, and Rim2) at the nanoscale in 2D. Next, we apply a targetable genetically-encoded electron microscopy labeling method that uses histidine based affinity-tags and metal-binding gold-nanoparticles to determine the 3D axial location of these exocytic proteins and two SNARE proteins (Syntaxin1A and SNAP25) using electron tomography. Rab proteins are distributed across the entire surface and t-SNARE proteins at the base of docked vesicles. We propose that the circumferential distribution of Rabs and Rab-effectors could aid in the efficient transport, capture, docking, and rapid fusion of calcium-triggered exocytic vesicles in excitable cells.

Indexed as

AnimalsCarbocyaninesCells, CulturedExocytosisGoldHeLa CellsHumansImaging, Three-DimensionalLuminescent ProteinsMetal NanoparticlesMicroscopyMolecular ImagingNeuroendocrine CellsPC12 Cellsrab GTP-Binding ProteinsRatsAlexa Fluor 647CarbocyaninesGoldLuminescent Proteinsrab GTP-Binding ProteinsRed Fluorescent ProteinSNARE ProteinsSytl4 protein, ratVesicular Transport Proteins

Identifiers

PMID34172739
PMCPMC8233335
OpenAlexW3173565824

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.