Evidence map›Paper›PMID 20045481›Full record

ReviewSeminars in cell & developmental biology2010

The PARL family of mitochondrial rhomboid proteases.

R Blake Hill, Luca Pellegrini

Abstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Regulation of mixotrophy inMicrobiology (Reading, England) · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Rhomboid family gene expression profiling in breast normal tissue and tumor samples.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Article
  7. PARL and HtrA2: another intricate ischemic neuronal apoptotic process starting within mitochondria.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2013
    Article
  8. The role of PARL and HtrA2 in striatal neuronal injury after transient global cerebral ischemia.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2013
    Article
  9. Structure and mechanism of rhomboid protease.The Journal of biological chemistry · 2013
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

2 authors.

R Blake HillDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA. hill@jhu.edu
Luca Pellegrini

Funding

Structural Biology of Mitochondrial FissionR01GM067180 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI HILL, R BLAKE · 2004 to 2022
$6.0M
CIHR MOP-82718NIGMS NIH HHS R01 GM067180NIGMS NIH HHS R01GM067180
6 · The paper itself

Abstract

Rhomboids are an ancient and conserved family of intramembrane-cleaving proteases, a small group of proteolytic enzymes capable of hydrolyzing a peptide bond within a transmembrane helix that anchors a substrate protein to the membrane. Mitochondrial rhomboids evolved in eukaryotes to coordinate a critical aspect of cell biology, the regulation of mitochondrial membranes dynamics. This function appears to have required the emergence of a structural feature that is unique among all other rhomboids: an additional transmembrane helix (TMH) positioned at the N-terminus of six TMHs that form the core proteolytic domain of all prokaryotic and eukaryotic rhomboids. This "1+6" structure, which is shared only among mitochondrial rhomboids, defines a subfamily of rhomboids with the prototypical family member being mammalian Parl. Here, we present the findings that in 11 years have elevated mitochondrial rhomboids as the gatekeepers of mitochondrial dynamics and apoptosis; further, we discuss the aspects of their biology that are bound to introduce new paradigm shifts in our understanding of how the organelle uses this unique type of protease to govern stress, signaling to the nucleus, and other key mitochondrial activities in health and disease.

Indexed as

AnimalsApoptosisHumansMetalloproteasesMitochondriaMitochondrial ProteinsModels, MolecularPeptide HydrolasesProtein ConformationSaccharomyces cerevisiae ProteinsSerine EndopeptidasesSignal TransductionSubstrate SpecificityMetalloproteasesMitochondrial ProteinsPARL protein, humanPcp1 protein, S cerevisiaePeptide HydrolasesSaccharomyces cerevisiae ProteinsSerine Endopeptidases

Identifiers

PMID20045481
PMCPMC2908206

What OpenQuestion holds

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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.