Evidence map›Paper›PMID 34546351›Full record

ArticleThe Journal of cell biology2021

The hypervariable region of atlastin-1 is a site for intrinsic and extrinsic regulation.

Carolyn M Kelly, Laura J Byrnes, Niharika Neela, Holger Sondermann, John P O'Donnell

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. The atlastin paralogs: The complexity in the tails.The Journal of cell biology · 2023
    Article
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 3 countries.

Carolyn M KellyDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY.ORCID 0000-0003-1006-5169
Laura J ByrnesDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY.
Niharika NeelaDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY.
Holger SondermannDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY.ORCID 0000-0003-2211-6234
John P O'DonnellDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY.ORCID 0000-0002-0571-3603
Cornell University · USMRC Laboratory of Molecular Biology · GB

Funding

Training and OutreachP30GM124166 · NIGMS · CORNELL UNIVERSITY · PI RICHARD A. CERIONE · 2019 to 2026
$28.3M
NIGMS NIH HHS GM-124166NIGMS NIH HHS P30 GM124166
6 · The paper itself

Abstract

Atlastin (ATL) GTPases catalyze homotypic membrane fusion of the peripheral endoplasmic reticulum (ER). GTP-hydrolysis-driven conformational changes and membrane tethering are prerequisites for proper membrane fusion. However, the molecular basis for regulation of these processes is poorly understood. Here we establish intrinsic and extrinsic modes of ATL1 regulation that involve the N-terminal hypervariable region (HVR) of ATLs. Crystal structures of ATL1 and ATL3 exhibit the HVR as a distinct, isoform-specific structural feature. Characterizing the functional role of ATL1's HVR uncovered its positive effect on membrane tethering and on ATL1's cellular function. The HVR is post-translationally regulated through phosphorylation-dependent modification. A kinase screen identified candidates that modify the HVR site specifically, corresponding to the modifications on ATL1 detected in cells. This work reveals how the HVR contributes to efficient and potentially regulated activity of ATLs, laying the foundation for the identification of cellular effectors of ATL-mediated membrane processes.

Indexed as

AnimalsCell LineEndoplasmic ReticulumGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateHumansHydrolysisMembrane FusionMembrane ProteinsMiceNIH 3T3 CellsProtein Processing, Post-TranslationalATL1 protein, humanGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateMembrane Proteins

Identifiers

PMID34546351
PMCPMC8563291
OpenAlexW3200797065

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.