Evidence map›Paper›PMID 23596323›Full record

ArticleMolecular biology of the cell2013

Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular recycling endosome biogenesis.

Sai Srinivas Panapakkam Giridharan, Bishuang Cai, Nicolas Vitale, Naava Naslavsky, Steve Caplan

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
5.5field-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

77 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  7. Review
  8. The endocytic fission protein EHD1 interacts with tubulin and regulates microtubule function.Biochimica et biophysica acta. Molecular cell research · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
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  16. Review
  17. Article
  18. Article
  19. PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022
    Review
  20. Article

17 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

5 authors at 2 institutions in 2 countries.

Sai Srinivas Panapakkam GiridharanDepartment of Biochemistry and Molecular Biology and Eppley Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198, USA.
Bishuang Cai
Nicolas Vitale
Naava Naslavsky
Steve Caplan
University of Nebraska Medical Center · USInstitut des Neurosciences Cellulaires et Intégratives · FR

Funding

Molecular Mechanisms Controlling Endocytic RecyclingR01GM074876 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H · 2006 to 2015
$2.6M
Nebraska Center for Cellular SignalingP20GM103489 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI JOHNSON, KEITH R · 2012 to 2012
$2.0M
Regulation of EHD protein function by molecular partner interactionsR01GM087455 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H, SORGEN, PAUL L · 2010 to 2013
$1.1M
NIGMS NIH HHS 5P20GM103489-10NIGMS NIH HHS P20 GM103489NIGMS NIH HHS R01 GM074876NIGMS NIH HHS R01 GM087455NIGMS NIH HHS R01GM087455
6 · The paper itself

Abstract

Endocytic transport necessitates the generation of membrane tubules and their subsequent fission to transport vesicles for sorting of cargo molecules. The endocytic recycling compartment, an array of tubular and vesicular membranes decorated by the Eps15 homology domain protein, EHD1, is responsible for receptor and lipid recycling to the plasma membrane. It has been proposed that EHD dimers bind and bend membranes, thus generating recycling endosome (RE) tubules. However, recent studies show that molecules interacting with CasL-Like1 (MICAL-L1), a second, recently identified RE tubule marker, recruits EHD1 to preexisting tubules. The mechanisms and events supporting the generation of tubular recycling endosomes were unclear. Here, we propose a mechanism for the biogenesis of RE tubules. We demonstrate that MICAL-L1 and the BAR-domain protein syndapin2 bind to phosphatidic acid, which we identify as a novel lipid component of RE. Our studies demonstrate that direct interactions between these two proteins stabilize their association with membranes, allowing for nucleation of tubules by syndapin2. Indeed, the presence of phosphatidic acid in liposomes enhances the ability of syndapin2 to tubulate membranes in vitro. Overall our results highlight a new role for phosphatidic acid in endocytic recycling and provide new insights into the mechanisms by which tubular REs are generated.

Indexed as

Adaptor Proteins, Signal TransducingBinding SitesBiological TransportCalponinsCell MembraneCytoskeletal ProteinsEndosomesGene ExpressionHeLa CellsHumansLIM Domain ProteinsMicrofilament ProteinsMixed Function OxygenasesPhosphatidic AcidsProtein BindingProtein Structure, TertiaryAdaptor Proteins, Signal TransducingCalponinsCytoskeletal ProteinsEHD1 protein, humanLIM Domain ProteinsMICAL1 protein, humanMicrofilament ProteinsMixed Function OxygenasesPACSIN2 protein, humanPhosphatidic AcidsVesicular Transport Proteins

Identifiers

PMID23596323
PMCPMC3667729
OpenAlexW2002007022

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.