Evidence map›Paper›PMID 27241910›Full record

ArticleThe Journal of cell biology2016

Num1 anchors mitochondria to the plasma membrane via two domains with different lipid binding specificities.

Holly A Ping, Lauren M Kraft, WeiTing Chen, Amy E Nilles, Laura L Lackner

Abstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
–field-weighted citation impact
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

51 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Cell membrane asymmetries and cellular aging.The Biochemical journal · 2025
    Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Imaging interorganelle contacts at a glance.Journal of cell science · 2024
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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.

Holly A PingDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208.
Lauren M KraftDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208.
WeiTing ChenDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208.
Amy E NillesDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208.
Laura L LacknerDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208 laura.lackner@northwestern.edu.

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
NCI NIH HHS P30 CA060553NIGMS NIH HHS T32 GM008061NIGMS NIH HHS T32 GM008382
6 · The paper itself

Abstract

The mitochondria-ER cortex anchor (MECA) is required for proper mitochondrial distribution and functions by tethering mitochondria to the plasma membrane. The core component of MECA is the multidomain protein Num1, which assembles into clusters at the cell cortex. We show Num1 adopts an extended, polarized conformation. Its N-terminal coiled-coil domain (Num1CC) is proximal to mitochondria, and the C-terminal pleckstrin homology domain is associated with the plasma membrane. We find that Num1CC interacts directly with phospholipid membranes and displays a strong preference for the mitochondria-specific phospholipid cardiolipin. This direct membrane interaction is critical for MECA function. Thus, mitochondrial anchoring is mediated by a protein that interacts directly with two different membranes through lipid-specific binding domains, suggesting a general mechanism for interorganelle tethering.

Indexed as

CardiolipinsCell MembraneCytoskeletal ProteinsEndoplasmic ReticulumLipidsMitochondriaMitochondrial MembranesMitochondrial ProteinsPhospholipidsProtein BindingProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipSubstrate SpecificityCardiolipinsCytoskeletal ProteinsLipidsMdm36 protein, S cerevisiaeMitochondrial ProteinsNUM1 protein, S cerevisiaePhospholipidsSaccharomyces cerevisiae Proteins

Identifiers

PMID27241910
PMCPMC4896055

What OpenQuestion holds

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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.