PELO

UniProt ID: Q9BRX2
Organism: Homo sapiens
Review Status: COMPLETE
πŸ“ Provide Detailed Feedback

Gene Description

PELO (Protein pelota homolog, the human ortholog of yeast Dom34) is a cytoplasmic ribosome-rescue factor of the eukaryotic release factor 1 (eRF1) family, Pelota subfamily. Structurally it mimics eRF1 and occupies the ribosomal A site, but it lacks the catalytic GGQ motif and therefore has no peptidyl-tRNA hydrolase (peptide-release) activity. PELO forms the Pelota-HBS1L complex (also called the Dom34-Hbs1 complex) with the translational GTPase HBS1L. This complex recognizes ribosomes that are stalled at the 3' end of an mRNA (truncated, non-stop, or no-go messages), engages the empty mRNA channel, and, after mRNA extraction by the SKI complex, recruits the recycling ATPase ABCE1 to split the stalled 80S ribosome into subunits. PELO thereby initiates the no-go decay (NGD) and non-stop decay (NSD) mRNA surveillance pathways and rescues stalled ribosomes. It is ubiquitously expressed and is also recruited, in a PINK1-regulated manner, to mitochondrially associated ribosomes during mitophagy.

Existing Annotations Review

GO Term Evidence Action Reason
GO:0022626 cytosolic ribosome
IBA
GO_REF:0000033
ACCEPT
Summary: PELO acts on the cytosolic 80S ribosome, where it occupies the A site of stalled ribosomes. Phylogenetic transfer agrees with direct cryo-EM evidence.
Reason: PELO's site of action is the cytosolic ribosome; supported by direct structural evidence of PELO bound to stalled ribosomes.
Supporting Evidence:
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
GO:0072344 rescue of stalled cytosolic ribosome
IBA
GO_REF:0000033
ACCEPT
Summary: Rescue of stalled ribosomes is the defining biological role of PELO. The IBA inference is corroborated by multiple direct experimental annotations.
Reason: Core biological process for PELO, supported by conserved function across yeast Dom34, Drosophila pelo and human PELO and by direct mammalian biochemistry.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway
GO:0170011 stalled ribosome sensor activity
IBA
GO_REF:0000033
ACCEPT
Summary: PELO senses ribosomes stalled at the 3' end of mRNA by probing the (near-)empty mRNA channel/A site, the molecular function underlying rescue. IBA agrees with direct IDA evidence.
Reason: This is PELO's core molecular function; phylogenetic inference is consistent with direct structural evidence.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
PELO recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel
GO:1990533 Dom34-Hbs1 complex
IBA
GO_REF:0000033
ACCEPT
Summary: PELO is one of the two subunits of the Dom34-Hbs1 (Pelota-HBS1L) complex. Phylogenetic assignment matches direct evidence.
Reason: PELO is a defining, conserved component of this complex.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
Component of the Pelota-HBS1L complex, also named Dom34-Hbs1 complex, composed of PELO and HBS1L
GO:0005737 cytoplasm
IEA
GO_REF:0000044
KEEP AS NON CORE
Summary: Electronic localization to the cytoplasm, consistent with the documented cytoplasmic site of action; less precise than the cytosolic ribosome annotation.
Reason: Correct but generic compartment annotation; the informative localization is the cytosolic ribosome / Dom34-Hbs1 complex.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
SUBCELLULAR LOCATION: Cytoplasm
GO:0070481 nuclear-transcribed mRNA catabolic process, non-stop decay
IEA
GO_REF:0000002
ACCEPT
Summary: PELO/HBS1L mediate non-stop decay by recognizing ribosomes that have read to the 3' end of an mRNA lacking a stop codon. Supported by direct experiment.
Reason: NSD is a genuine PELO process; the InterPro IEA is corroborated by direct evidence in mammalian cells.
Supporting Evidence:
PMID:23667253
The Hbs1-Dom34 protein complex functions in non-stop mRNA decay in mammalian cells
GO:0070966 nuclear-transcribed mRNA catabolic process, no-go decay
IEA
GO_REF:0000002
ACCEPT
Summary: No-go decay is triggered by PELO recognition of stalled ribosomes. The InterPro IEA duplicates better-supported IDA annotations.
Reason: NGD is a core PELO process, supported by direct experimental annotations.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway
GO:0071025 RNA surveillance
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: General mRNA surveillance term; NGD/NSD are the specific PELO surveillance pathways already captured by more precise terms.
Reason: Correct but a parent of the specific no-go/non-stop decay terms; retained as a less-informative general annotation.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway
GO:0005515 protein binding
IPI
PMID:20406461
Pelota interacts with HAX1, EIF3G and SRPX and the resulting...
KEEP AS NON CORE
Summary: High-throughput IntAct interactions (e.g. EIF3G, HAX1, SRPX). Bare protein binding is uninformative; EIF3G is a plausible translation-related partner but not part of the defined complex.
Reason: Records real physical interactions but the generic protein binding term adds nothing to PELO's defined ribosome-rescue function.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
O75821: EIF3G
GO:0005515 protein binding
IPI
PMID:25277244
The functional landscape of Hsp27 reveals new cellular proce...
KEEP AS NON CORE
Summary: IntAct interaction with HSPB1 (P04792). Bare protein binding; isolated chaperone interaction not central to ribosome rescue.
Reason: Generic protein binding from a single interaction; uninformative for core function.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
P04792: HSPB1
GO:0005515 protein binding
IPI
PMID:25416956
A proteome-scale map of the human interactome network.
KEEP AS NON CORE
Summary: Yeast two-hybrid interactome capturing the PELO-HBS1L interaction, the one biologically meaningful partner here.
Reason: The bare term is uninformative, but the HBS1L partner is the defining one; the functional consequence (Dom34-Hbs1 complex) is captured by GO:1990533.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
Q9Y450: HBS1L
GO:0005515 protein binding
IPI
PMID:31515488
Extensive disruption of protein interactions by genetic vari...
KEEP AS NON CORE
Summary: Interactome screen again capturing PELO-HBS1L. Generic term but relevant partner.
Reason: Confirms the HBS1L interaction; bare protein binding term is non-core.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
Q9Y450: HBS1L
GO:0005515 protein binding
IPI
PMID:32296183
A reference map of the human binary protein interactome.
KEEP AS NON CORE
Summary: Binary interactome map including HBS1L plus various non-specific partners (DYNLT1, LMO3/4, MEOX2, etc.). Bare protein binding.
Reason: Mixed interactor set; only HBS1L is functionally relevant and is already captured by the complex annotation.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
Q9Y450: HBS1L
GO:0005515 protein binding
IPI
PMID:32814053
Interactome Mapping Provides a Network of Neurodegenerative ...
KEEP AS NON CORE
Summary: Neurodegeneration interactome screen capturing many high-throughput partners (HTT, FLNA, NEFL, BAG3, etc.) unrelated to PELO's defined function.
Reason: Large set of isolated high-throughput interactions with no clear link to ribosome rescue; bare protein binding term is uninformative.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
P42858: HTT
GO:0005829 cytosol
TAS
Reactome:R-HSA-9954730
KEEP AS NON CORE
Summary: Reactome curated cytosolic localization in ribosome-rescue reactions, consistent with PELO's site of action.
Reason: Correct localization but generic; the cytosolic ribosome / complex annotations are more informative.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
SUBCELLULAR LOCATION: Cytoplasm
GO:0005829 cytosol
TAS
Reactome:R-HSA-9954919
KEEP AS NON CORE
Summary: Reactome curated cytosolic localization (duplicate context).
Reason: Correct but generic localization, redundant with other cytosol annotations.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
SUBCELLULAR LOCATION: Cytoplasm
GO:0005829 cytosol
TAS
Reactome:R-HSA-9955731
KEEP AS NON CORE
Summary: Reactome curated cytosolic localization (duplicate context).
Reason: Correct but generic localization, redundant with other cytosol annotations.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
SUBCELLULAR LOCATION: Cytoplasm
GO:0022626 cytosolic ribosome
IDA
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTP...
ACCEPT
Summary: Direct cryo-EM evidence places PELO on the stalled cytosolic 80S ribosome.
Reason: Strong direct structural evidence for PELO acting on the cytosolic ribosome.
Supporting Evidence:
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
GO:0170011 stalled ribosome sensor activity
IDA
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTP...
ACCEPT
Summary: Direct structural/biochemical demonstration that PELO senses the stalled-ribosome state via the mRNA channel. Core molecular function.
Reason: Best-supported molecular function for PELO; direct IDA evidence.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
PELO recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel
GO:0032790 ribosome disassembly
IDA
PMID:21448132
Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 8...
ACCEPT
Summary: With HBS1L and ABCE1, PELO drives dissociation of 80S ribosomes into subunits, demonstrated by in vitro reconstitution.
Reason: Directly demonstrated; ribosome disassembly (subunit splitting) is the mechanistic output of PELO-mediated rescue.
Supporting Evidence:
PMID:21448132
Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
GO:0043022 ribosome binding
IDA
PMID:27543824
Conserved functions of human Pelota in mRNA quality control ...
ACCEPT
Summary: PELO binds the ribosome; the K2A and R45A mutants that abolish rescue map to the ribosome/mRNA-channel-engaging surface.
Reason: Directly demonstrated ribosome binding underlying rescue activity.
Supporting Evidence:
PMID:27543824
Conserved functions of human Pelota in mRNA quality control of nonstop mRNA
GO:0043022 ribosome binding
IDA
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTP...
ACCEPT
Summary: Cryo-EM directly shows PELO bound to the stalled ribosome.
Reason: Direct structural evidence of ribosome binding.
Supporting Evidence:
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
GO:0070966 nuclear-transcribed mRNA catabolic process, no-go decay
IDA
PMID:23667253
The Hbs1-Dom34 protein complex functions in non-stop mRNA de...
ACCEPT
Summary: PELO/HBS1L drive no-go/non-stop decay of aberrant mRNAs in mammalian cells.
Reason: Directly demonstrated NGD role.
Supporting Evidence:
PMID:23667253
The Hbs1-Dom34 protein complex functions in non-stop mRNA decay in mammalian cells
GO:0070966 nuclear-transcribed mRNA catabolic process, no-go decay
IDA
PMID:27543824
Conserved functions of human Pelota in mRNA quality control ...
ACCEPT
Summary: Human Pelota functions in mRNA quality control of nonstop mRNA; loss-of-function mutants abolish activity.
Reason: Direct mutagenesis-supported evidence for PELO in no-go/non-stop mRNA decay.
Supporting Evidence:
PMID:27543824
Conserved functions of human Pelota in mRNA quality control of nonstop mRNA
GO:0070966 nuclear-transcribed mRNA catabolic process, no-go decay
IDA
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTP...
ACCEPT
Summary: Structural study supporting PELO's role in recognizing stalled ribosomes that triggers no-go decay.
Reason: Direct evidence for the NGD-triggering recognition step.
Supporting Evidence:
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
GO:0072344 rescue of stalled cytosolic ribosome
IDA
PMID:21448132
Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 8...
ACCEPT
Summary: In vitro reconstitution shows PELO (with HBS1L/ABCE1) rescues stalled elongation complexes. Core process.
Reason: Directly demonstrated core biological process of PELO.
Supporting Evidence:
PMID:21448132
Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
GO:0072344 rescue of stalled cytosolic ribosome
IDA
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTP...
ACCEPT
Summary: Structural demonstration of PELO engaging stalled ribosomes for rescue.
Reason: Direct structural evidence for the core rescue process.
Supporting Evidence:
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
GO:1990533 Dom34-Hbs1 complex
IDA
PMID:27863242
Decoding Mammalian Ribosome-mRNA States by Translational GTP...
ACCEPT
Summary: PELO directly identified as a component of the Pelota-HBS1L (Dom34-Hbs1) complex by cryo-EM.
Reason: Direct evidence for PELO as a complex subunit.
Supporting Evidence:
file:human/PELO/PELO-uniprot.txt
Component of the Pelota-HBS1L complex, also named Dom34-Hbs1 complex, composed of PELO and HBS1L

Core Functions

Stalled-ribosome sensor / eRF1-like factor that recognizes ribosomes stalled at the 3' end of an mRNA by probing the empty mRNA channel and A site, the molecular recognition event that initiates ribosome rescue. Unlike eRF1, PELO lacks peptidyl-tRNA hydrolase activity.

Cellular Locations:
Supporting Evidence:
  • file:human/PELO/PELO-uniprot.txt
    PELO recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel

As the eRF1-like subunit of the Pelota-HBS1L (Dom34-Hbs1) complex, with the GTPase HBS1L and recycling ATPase ABCE1, PELO rescues stalled ribosomes by driving their dissociation into subunits, initiating no-go and non-stop mRNA decay.

Molecular Function:
ribosome binding
Supporting Evidence:
  • PMID:21448132
    Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
  • file:human/PELO/PELO-uniprot.txt
    Component of the Pelota-HBS1L complex, also named Dom34-Hbs1 complex, composed of PELO and HBS1L

References

Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Pelota interacts with HAX1, EIF3G and SRPX and the resulting protein complexes are associated with the actin cytoskeleton.
Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes.
  • Pelota, Hbs1 and ABCE1 together dissociate vacant 80S ribosomes and stalled elongation complexes into subunits.
The Hbs1-Dom34 protein complex functions in non-stop mRNA decay in mammalian cells.
  • The mammalian Hbs1-Dom34 (HBS1L-PELO) complex functions in non-stop mRNA decay.
The functional landscape of Hsp27 reveals new cellular processes such as DNA repair and alternative splicing and proposes novel anticancer targets.
A proteome-scale map of the human interactome network.
Conserved functions of human Pelota in mRNA quality control of nonstop mRNA.
  • Human Pelota functions in mRNA quality control of nonstop mRNA; the K2A and R45A mutants abolish its ability to rescue stalled ribosomes.
Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.
  • Cryo-EM of the PELO-HBS1L complex on stalled ribosomes defines PELO's stalled-ribosome sensor activity and ribosome binding.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Reactome:R-HSA-9954730
Reactome ribosome quality control reaction (PELO cytosol)
Reactome:R-HSA-9954919
Reactome ribosome quality control reaction (PELO cytosol)
Reactome:R-HSA-9955731
Reactome ribosome quality control reaction (PELO cytosol)

Suggested Questions for Experts

Q: How is the choice between productive translation termination (eRF1) and rescue (PELO) made at ribosomes with short or empty mRNA in the channel?

Q: What is the in vivo contribution of the PINK1-regulated PELO recruitment to mitochondrial ribosomes relative to its canonical cytosolic rescue role?

Suggested Experiments

Experiment: Ribosome profiling and 5'P degradome sequencing in PELO-knockout versus wild-type human cells to quantify accumulation of stalled/truncated mRNAs and define the endogenous no-go/non-stop substrate repertoire.

Experiment: Reconstituted single-molecule or cryo-EM time-resolved analysis of PELO-HBS1L-ABCE1 splitting kinetics on defined stalled substrates to dissect the mRNA-channel sensing step.

πŸ“š Additional Documentation

Notes

(PELO-notes.md)

PELO (Pelota homolog / Dom34) β€” research notes

UniProt: Q9BRX2. Member of the eukaryotic release factor 1 (eRF1) family, Pelota subfamily. 385 aa, cytoplasmic.

Core function

PELO is the eRF1-like component of the Pelota-HBS1L (Dom34-Hbs1) complex, a ribosome-rescue
machine. Unlike eRF1, it has no peptidyl-tRNA hydrolase (peptide release) activity; it instead
recognizes ribosomes stalled at the 3' end of an mRNA (truncated/non-stop, no-go) and, together
with the GTPase HBS1L and the recycling ATPase ABCE1, drives subunit dissociation (ribosome
disassembly), initiating No-Go Decay (NGD) and Non-Stop Decay (NSD).

  • [file:human/PELO/PELO-uniprot.txt "Component of the Pelota-HBS1L complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway"]
  • [file:human/PELO/PELO-uniprot.txt "In the Pelota-HBS1L complex, PELO recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel"]
  • [file:human/PELO/PELO-uniprot.txt "Belongs to the eukaryotic release factor 1 family. Pelota subfamily."]
  • PMID:21448132 β€” biochemical reconstitution of subunit dissociation (ribosome disassembly).
  • PMID:27863242 β€” cryo-EM of the PELO-HBS1L complex on stalled ribosomes; defines stalled-ribosome sensor activity, ribosome binding, Dom34-Hbs1 complex.
  • PMID:23667253 β€” NSD/no-go decay role.
  • PMID:27543824 β€” K2A/R45A mutants abolish rescue of stalled ribosomes (UniProt MUTAGEN).

Other / non-core

  • PINK1-regulated mitophagy: upon mitochondrial damage PELO is recruited to mito-OM-associated ribosome/mRNP, enabling autophagy receptor recruitment PMID:29861391. Peripheral, context-specific.
  • Many IntAct protein binding IPI rows are high-throughput interactors (HSPB1, HTT, FLNA, etc.); HBS1L (Q9Y450) and EIF3G/ABCE1 are the biologically meaningful ones. Bare GO:0005515 is uninformative.
  • Ensembl IEA developmental terms (endoderm development, inner cell mass proliferation, BMP signaling, stem cell maintenance) reflect mouse Pelo knockout phenotypes (embryonic lethality) β€” downstream/pleiotropic, not in GOA TSV here.

Action plan

  • Core MF: GO:0170011 stalled ribosome sensor activity; GO:0043022 ribosome binding. Core BP: GO:0072344 rescue of stalled cytosolic ribosome; GO:0032790 ribosome disassembly. Core CC: GO:1990533 Dom34-Hbs1 complex.
  • NGD/NSD BP (GO:0070966, GO:0070481) accept/keep.
  • Bare protein binding IPI β†’ KEEP_AS_NON_CORE (HBS1L) or MARK_AS_OVER_ANNOTATED (random HT hits).

Pn Notes

(PELO-pn-notes.md)

PELO PN Consistency Notes

  • Generated: 2026-06-18
  • Project: PROTEOSTASIS
  • Scope: PN consistency rereview against local AIGR review and available deep-research artifacts
  • UniProt: Q9BRX2
  • AIGR review status: COMPLETE
  • Review batch: proteostasis-batch-2026-06-07c
  • Batch change status: added

Source Files Checked

Deep Research Files

  • No *-deep-research*.md file found in this gene directory.

AIGR Review Snapshot

  • Description: PELO (Protein pelota homolog, the human ortholog of yeast Dom34) is a cytoplasmic ribosome-rescue factor of the eukaryotic release factor 1 (eRF1) family, Pelota subfamily. Structurally it mimics eRF1 and occupies the ribosomal A site, but it lacks the catalytic GGQ motif and therefore has no peptidyl-tRNA hydrolase (peptide-release) activity. PELO forms the Pelota-HBS1L complex (also called the Dom34-Hbs1 complex) with the translational GTPase HBS1L. This complex recognizes ribosomes that are stalled at the 3' end of an mRNA (truncated, non-stop, or no-go messages), engages the empty mRNA channel, and, after mRNA extraction by the SKI complex, recruits the recycling ATPase ABCE1 to split the stalled 80S ribosome into subunits. PELO thereby initiates the no-go decay (NGD) and non-stop decay (NSD) mRNA surveillance pathways and rescues stalled ribosomes. It is ubiquitously expressed and is also recruited, in a PINK1-regulated manner, to mitochondrially associated ribosomes during mitophagy.
  • Existing/core annotation action counts: ACCEPT: 17; KEEP_AS_NON_CORE: 11

PN Consistency Summary

  • Consistency: Excellent across all four sources. Deep research, notes, review, PN and GOA all agree PELO is the eRF1-like ribosome-rescue factor (Pelota subfamily; no GGQ/peptidyl-tRNA hydrolase), subunit of the Pelota-HBS1L (Dom34-Hbs1) complex, working with HBS1L+ABCE1 to split stalled 80S and initiate NGD/NSD. No contradictions.
  • PN story / NEW pressure: GO:0072344 (verified real, rescue of stalled cytosolic ribosome) is already in GOA and in the review (IDA PMID:21448132, 27863242 + IBA) β€” fully captured. GO:0006515 (verified real) is new_to_goa; PELO genuinely drives stalled-ribosome QC, so it is a defensible higher-level process ADD, but it is broader than the review's already-precise GO:0072344/GO:0032790/GO:0070966/GO:0070481 set. Conclude: rescue already captured; GO:0006515 a defensible but redundant (broader) ADD.
  • Evidence alignment: PN cites no PMIDs (row had none). Review evidence (21448132, 23667253, 27543824, 27863242) is fully self-consistent and HIGH/VERIFIED. No divergence to reconcile.
  • Verdict: Fully consistent; PN rescue mapping already captured exactly (GO:0072344), GO:0006515 is a defensible-but-broader ADD already entailed by finer terms. No YAML change needed.

Full Consistency Review

  • UniProt: Q9BRX2 Β· batch: proteostasis-batch-2026-06-07c Β· review status: COMPLETE (clean; all ACCEPT or KEEP_AS_NON_CORE)
  • PN placement: 1 row β€” Translation|Cytosolic translation|Ribosome-associated QC|Ribosomal rescue. PN-node mapping: rescue-typeβ†’mapped GO:0072344 rescue of stalled cytosolic ribosome (already_in_goa_exact); RQC-groupβ†’mapped GO:0006515 protein QC (new_to_goa); class/branch context_only. Projected: GO:0072344 (already in GOA), GO:0006515 (new).
  • Consistency: Excellent across all four sources. Deep research, notes, review, PN and GOA all agree PELO is the eRF1-like ribosome-rescue factor (Pelota subfamily; no GGQ/peptidyl-tRNA hydrolase), subunit of the Pelota-HBS1L (Dom34-Hbs1) complex, working with HBS1L+ABCE1 to split stalled 80S and initiate NGD/NSD. No contradictions.
  • PN story / NEW pressure: GO:0072344 (verified real, rescue of stalled cytosolic ribosome) is already in GOA and in the review (IDA PMID:21448132, 27863242 + IBA) β€” fully captured. GO:0006515 (verified real) is new_to_goa; PELO genuinely drives stalled-ribosome QC, so it is a defensible higher-level process ADD, but it is broader than the review's already-precise GO:0072344/GO:0032790/GO:0070966/GO:0070481 set. Conclude: rescue already captured; GO:0006515 a defensible but redundant (broader) ADD.
  • Mapping strategy: Does not change the node. PN rescue-typeβ†’GO:0072344 exactly matches the review's core BP. The groupβ†’GO:0006515 propagation is broader than (a parent of) terms already annotated; per the TOMM20/HSPA8/RAB7A "rejected as broader" precedent it adds little. Status/scope (mapped, ok_for_propagation) are appropriate at the type level.
  • Evidence alignment: PN cites no PMIDs (row had none). Review evidence (21448132, 23667253, 27543824, 27863242) is fully self-consistent and HIGH/VERIFIED. No divergence to reconcile.
  • Verdict: Fully consistent; PN rescue mapping already captured exactly (GO:0072344), GO:0006515 is a defensible-but-broader ADD already entailed by finer terms. No YAML change needed.
  • Recommended edits: none required. [MAP] (optional) treat GO:0006515 for PELO as broader/redundant given GO:0072344 already exact in GOA+review.

PN Dossier Context

  • review_batch: proteostasis-batch-2026-06-07c
  • review_yaml: genes/human/PELO/PELO-ai-review.yaml
  • PN workbook rows: 1

PN row 1: Translation | Cytosolic translation | Ribosome-associated QC | Ribosomal rescue

  • UniProt: Q9BRX2
  • In branches: TR
  • PN-node mapping records (path + ancestors):
    • [type] Translation|Cytosolic translation|Ribosome-associated QC|Ribosomal rescue
      status=mapped scope=ok_for_propagation_to_go GO=[GO:0072344 rescue of stalled cytosolic ribosome]
      rationale: This PN RQC type denotes rescue of stalled cytosolic ribosomes. The matching GO process term is the direct target.
    • [group] Translation|Cytosolic translation|Ribosome-associated QC
      status=mapped scope=ok_for_propagation_to_go GO=[GO:0006515 protein quality control for misfolded or incompletely synthesized proteins]
      rationale: The PN ribosome-associated quality-control group covers surveillance and disposal of stalled or defective nascent-chain translation products. GO lacks a dedicated ribosome-associated QC term in the local cache, so the broader protein-quality-control process is the best supported target.
    • [class] Translation|Cytosolic translation
      status=context_only scope=too_broad_to_propagate GO=[GO:0002181 cytoplasmic translation]
      rationale: The PN class Cytosolic translation is centered on the cytoplasmic translation apparatus and process, but it also houses supporting machinery such as ribosome biogenesis factors. The GO process term is a useful high-level label for the class, but propagating it to all members would over-annotate genes whose PN placement is through assembly or maturation context rather than core cytoplasmic translation.
    • [branch] Translation
      status=context_only scope=too_broad_to_propagate GO=[GO:0006412 translation]
      rationale: The PN Translation branch is organized around the translation apparatus and immediately associated cotranslational quality-control systems. GO translation is the closest high-level process label, but the PN branch also contains adjacent machinery such as ribosome biogenesis and nascent-chain handling. Keeping this relationship is useful for interpretation, but it is too broad to project safely onto every member.

Projected GO annotations (2)

  • GO:0006515 protein quality control for misfolded or incompletely synthesized proteins | scope=ok_for_propagation_to_go | goa_status=new_to_goa | from=Translation|Cytosolic translation|Ribosome-associated QC
  • GO:0072344 rescue of stalled cytosolic ribosome | scope=ok_for_propagation_to_go | goa_status=already_in_goa_exact | from=Translation|Cytosolic translation|Ribosome-associated QC|Ribosomal rescue

Note

This file is generated from the current PROTEOSTASIS phase-1 dossier and local gene-review artifacts. Edit the source review, PN mapping, or dossier rather than this generated note when correcting the underlying curation.

πŸ“„ View Raw YAML

id: Q9BRX2
gene_symbol: PELO
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: PELO (Protein pelota homolog, the human ortholog of yeast Dom34) is a cytoplasmic ribosome-rescue factor of the eukaryotic release factor 1 (eRF1) family, Pelota subfamily. Structurally it mimics eRF1 and occupies the ribosomal A site, but it lacks the catalytic GGQ motif and therefore has no peptidyl-tRNA hydrolase (peptide-release) activity. PELO forms the Pelota-HBS1L complex (also called the Dom34-Hbs1 complex) with the translational GTPase HBS1L. This complex recognizes ribosomes that are stalled at the 3' end of an mRNA (truncated, non-stop, or no-go messages), engages the empty mRNA channel, and, after mRNA extraction by the SKI complex, recruits the recycling ATPase ABCE1 to split the stalled 80S ribosome into subunits. PELO thereby initiates the no-go decay (NGD) and non-stop decay (NSD) mRNA surveillance pathways and rescues stalled ribosomes. It is ubiquitously expressed and is also recruited, in a PINK1-regulated manner, to mitochondrially associated ribosomes during mitophagy.
existing_annotations:
- term:
    id: GO:0022626
    label: cytosolic ribosome
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: PELO acts on the cytosolic 80S ribosome, where it occupies the A site of stalled ribosomes. Phylogenetic transfer agrees with direct cryo-EM evidence.
    action: ACCEPT
    reason: PELO's site of action is the cytosolic ribosome; supported by direct structural evidence of PELO bound to stalled ribosomes.
    supported_by:
    - reference_id: PMID:27863242
      supporting_text: Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
- term:
    id: GO:0072344
    label: rescue of stalled cytosolic ribosome
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Rescue of stalled ribosomes is the defining biological role of PELO. The IBA inference is corroborated by multiple direct experimental annotations.
    action: ACCEPT
    reason: Core biological process for PELO, supported by conserved function across yeast Dom34, Drosophila pelo and human PELO and by direct mammalian biochemistry.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway
- term:
    id: GO:0170011
    label: stalled ribosome sensor activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: PELO senses ribosomes stalled at the 3' end of mRNA by probing the (near-)empty mRNA channel/A site, the molecular function underlying rescue. IBA agrees with direct IDA evidence.
    action: ACCEPT
    reason: This is PELO's core molecular function; phylogenetic inference is consistent with direct structural evidence.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: PELO recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel
- term:
    id: GO:1990533
    label: Dom34-Hbs1 complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  review:
    summary: PELO is one of the two subunits of the Dom34-Hbs1 (Pelota-HBS1L) complex. Phylogenetic assignment matches direct evidence.
    action: ACCEPT
    reason: PELO is a defining, conserved component of this complex.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: Component of the Pelota-HBS1L complex, also named Dom34-Hbs1 complex, composed of PELO and HBS1L
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Electronic localization to the cytoplasm, consistent with the documented cytoplasmic site of action; less precise than the cytosolic ribosome annotation.
    action: KEEP_AS_NON_CORE
    reason: Correct but generic compartment annotation; the informative localization is the cytosolic ribosome / Dom34-Hbs1 complex.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm'
- term:
    id: GO:0070481
    label: nuclear-transcribed mRNA catabolic process, non-stop decay
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: PELO/HBS1L mediate non-stop decay by recognizing ribosomes that have read to the 3' end of an mRNA lacking a stop codon. Supported by direct experiment.
    action: ACCEPT
    reason: NSD is a genuine PELO process; the InterPro IEA is corroborated by direct evidence in mammalian cells.
    supported_by:
    - reference_id: PMID:23667253
      supporting_text: The Hbs1-Dom34 protein complex functions in non-stop mRNA decay in mammalian cells
- term:
    id: GO:0070966
    label: nuclear-transcribed mRNA catabolic process, no-go decay
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: No-go decay is triggered by PELO recognition of stalled ribosomes. The InterPro IEA duplicates better-supported IDA annotations.
    action: ACCEPT
    reason: NGD is a core PELO process, supported by direct experimental annotations.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway
- term:
    id: GO:0071025
    label: RNA surveillance
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: General mRNA surveillance term; NGD/NSD are the specific PELO surveillance pathways already captured by more precise terms.
    action: KEEP_AS_NON_CORE
    reason: Correct but a parent of the specific no-go/non-stop decay terms; retained as a less-informative general annotation.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:20406461
  qualifier: enables
  review:
    summary: High-throughput IntAct interactions (e.g. EIF3G, HAX1, SRPX). Bare protein binding is uninformative; EIF3G is a plausible translation-related partner but not part of the defined complex.
    action: KEEP_AS_NON_CORE
    reason: Records real physical interactions but the generic protein binding term adds nothing to PELO's defined ribosome-rescue function.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'O75821: EIF3G'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25277244
  qualifier: enables
  review:
    summary: IntAct interaction with HSPB1 (P04792). Bare protein binding; isolated chaperone interaction not central to ribosome rescue.
    action: KEEP_AS_NON_CORE
    reason: Generic protein binding from a single interaction; uninformative for core function.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'P04792: HSPB1'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25416956
  qualifier: enables
  review:
    summary: Yeast two-hybrid interactome capturing the PELO-HBS1L interaction, the one biologically meaningful partner here.
    action: KEEP_AS_NON_CORE
    reason: The bare term is uninformative, but the HBS1L partner is the defining one; the functional consequence (Dom34-Hbs1 complex) is captured by GO:1990533.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'Q9Y450: HBS1L'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:31515488
  qualifier: enables
  review:
    summary: Interactome screen again capturing PELO-HBS1L. Generic term but relevant partner.
    action: KEEP_AS_NON_CORE
    reason: Confirms the HBS1L interaction; bare protein binding term is non-core.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'Q9Y450: HBS1L'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  qualifier: enables
  review:
    summary: Binary interactome map including HBS1L plus various non-specific partners (DYNLT1, LMO3/4, MEOX2, etc.). Bare protein binding.
    action: KEEP_AS_NON_CORE
    reason: Mixed interactor set; only HBS1L is functionally relevant and is already captured by the complex annotation.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'Q9Y450: HBS1L'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32814053
  qualifier: enables
  review:
    summary: Neurodegeneration interactome screen capturing many high-throughput partners (HTT, FLNA, NEFL, BAG3, etc.) unrelated to PELO's defined function.
    action: KEEP_AS_NON_CORE
    reason: Large set of isolated high-throughput interactions with no clear link to ribosome rescue; bare protein binding term is uninformative.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'P42858: HTT'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9954730
  qualifier: located_in
  review:
    summary: Reactome curated cytosolic localization in ribosome-rescue reactions, consistent with PELO's site of action.
    action: KEEP_AS_NON_CORE
    reason: Correct localization but generic; the cytosolic ribosome / complex annotations are more informative.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9954919
  qualifier: located_in
  review:
    summary: Reactome curated cytosolic localization (duplicate context).
    action: KEEP_AS_NON_CORE
    reason: Correct but generic localization, redundant with other cytosol annotations.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9955731
  qualifier: located_in
  review:
    summary: Reactome curated cytosolic localization (duplicate context).
    action: KEEP_AS_NON_CORE
    reason: Correct but generic localization, redundant with other cytosol annotations.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm'
- term:
    id: GO:0022626
    label: cytosolic ribosome
  evidence_type: IDA
  original_reference_id: PMID:27863242
  qualifier: is_active_in
  review:
    summary: Direct cryo-EM evidence places PELO on the stalled cytosolic 80S ribosome.
    action: ACCEPT
    reason: Strong direct structural evidence for PELO acting on the cytosolic ribosome.
    supported_by:
    - reference_id: PMID:27863242
      supporting_text: Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
- term:
    id: GO:0170011
    label: stalled ribosome sensor activity
  evidence_type: IDA
  original_reference_id: PMID:27863242
  qualifier: enables
  review:
    summary: Direct structural/biochemical demonstration that PELO senses the stalled-ribosome state via the mRNA channel. Core molecular function.
    action: ACCEPT
    reason: Best-supported molecular function for PELO; direct IDA evidence.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: PELO recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel
- term:
    id: GO:0032790
    label: ribosome disassembly
  evidence_type: IDA
  original_reference_id: PMID:21448132
  qualifier: involved_in
  review:
    summary: With HBS1L and ABCE1, PELO drives dissociation of 80S ribosomes into subunits, demonstrated by in vitro reconstitution.
    action: ACCEPT
    reason: Directly demonstrated; ribosome disassembly (subunit splitting) is the mechanistic output of PELO-mediated rescue.
    supported_by:
    - reference_id: PMID:21448132
      supporting_text: Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
- term:
    id: GO:0043022
    label: ribosome binding
  evidence_type: IDA
  original_reference_id: PMID:27543824
  qualifier: enables
  review:
    summary: PELO binds the ribosome; the K2A and R45A mutants that abolish rescue map to the ribosome/mRNA-channel-engaging surface.
    action: ACCEPT
    reason: Directly demonstrated ribosome binding underlying rescue activity.
    supported_by:
    - reference_id: PMID:27543824
      supporting_text: Conserved functions of human Pelota in mRNA quality control of nonstop mRNA
- term:
    id: GO:0043022
    label: ribosome binding
  evidence_type: IDA
  original_reference_id: PMID:27863242
  qualifier: enables
  review:
    summary: Cryo-EM directly shows PELO bound to the stalled ribosome.
    action: ACCEPT
    reason: Direct structural evidence of ribosome binding.
    supported_by:
    - reference_id: PMID:27863242
      supporting_text: Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
- term:
    id: GO:0070966
    label: nuclear-transcribed mRNA catabolic process, no-go decay
  evidence_type: IDA
  original_reference_id: PMID:23667253
  qualifier: involved_in
  review:
    summary: PELO/HBS1L drive no-go/non-stop decay of aberrant mRNAs in mammalian cells.
    action: ACCEPT
    reason: Directly demonstrated NGD role.
    supported_by:
    - reference_id: PMID:23667253
      supporting_text: The Hbs1-Dom34 protein complex functions in non-stop mRNA decay in mammalian cells
- term:
    id: GO:0070966
    label: nuclear-transcribed mRNA catabolic process, no-go decay
  evidence_type: IDA
  original_reference_id: PMID:27543824
  qualifier: involved_in
  review:
    summary: Human Pelota functions in mRNA quality control of nonstop mRNA; loss-of-function mutants abolish activity.
    action: ACCEPT
    reason: Direct mutagenesis-supported evidence for PELO in no-go/non-stop mRNA decay.
    supported_by:
    - reference_id: PMID:27543824
      supporting_text: Conserved functions of human Pelota in mRNA quality control of nonstop mRNA
- term:
    id: GO:0070966
    label: nuclear-transcribed mRNA catabolic process, no-go decay
  evidence_type: IDA
  original_reference_id: PMID:27863242
  qualifier: involved_in
  review:
    summary: Structural study supporting PELO's role in recognizing stalled ribosomes that triggers no-go decay.
    action: ACCEPT
    reason: Direct evidence for the NGD-triggering recognition step.
    supported_by:
    - reference_id: PMID:27863242
      supporting_text: Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
- term:
    id: GO:0072344
    label: rescue of stalled cytosolic ribosome
  evidence_type: IDA
  original_reference_id: PMID:21448132
  qualifier: involved_in
  review:
    summary: In vitro reconstitution shows PELO (with HBS1L/ABCE1) rescues stalled elongation complexes. Core process.
    action: ACCEPT
    reason: Directly demonstrated core biological process of PELO.
    supported_by:
    - reference_id: PMID:21448132
      supporting_text: Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
- term:
    id: GO:0072344
    label: rescue of stalled cytosolic ribosome
  evidence_type: IDA
  original_reference_id: PMID:27863242
  qualifier: involved_in
  review:
    summary: Structural demonstration of PELO engaging stalled ribosomes for rescue.
    action: ACCEPT
    reason: Direct structural evidence for the core rescue process.
    supported_by:
    - reference_id: PMID:27863242
      supporting_text: Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes
- term:
    id: GO:1990533
    label: Dom34-Hbs1 complex
  evidence_type: IDA
  original_reference_id: PMID:27863242
  qualifier: part_of
  review:
    summary: PELO directly identified as a component of the Pelota-HBS1L (Dom34-Hbs1) complex by cryo-EM.
    action: ACCEPT
    reason: Direct evidence for PELO as a complex subunit.
    supported_by:
    - reference_id: file:human/PELO/PELO-uniprot.txt
      supporting_text: Component of the Pelota-HBS1L complex, also named Dom34-Hbs1 complex, composed of PELO and HBS1L
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
  findings: []
- id: PMID:20406461
  title: Pelota interacts with HAX1, EIF3G and SRPX and the resulting protein complexes are associated with the actin cytoskeleton.
  findings: []
- id: PMID:21448132
  title: Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes.
  findings:
  - statement: Pelota, Hbs1 and ABCE1 together dissociate vacant 80S ribosomes and stalled elongation complexes into subunits.
    reference_section_type: RESULTS
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Cached publication title matches; establishes the PELO-HBS1L-ABCE1 ribosome dissociation/recycling activity (anchors GO:0043022 ribosome binding IDA in GOA).
- id: PMID:23667253
  title: The Hbs1-Dom34 protein complex functions in non-stop mRNA decay in mammalian cells.
  findings:
  - statement: The mammalian Hbs1-Dom34 (HBS1L-PELO) complex functions in non-stop mRNA decay.
    reference_section_type: RESULTS
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Cached publication title matches; establishes PELO-HBS1L role in non-stop mRNA decay (GO:0070966).
- id: PMID:25277244
  title: The functional landscape of Hsp27 reveals new cellular processes such as DNA repair and alternative splicing and proposes novel anticancer targets.
  findings: []
- id: PMID:25416956
  title: A proteome-scale map of the human interactome network.
  findings: []
- id: PMID:27543824
  title: Conserved functions of human Pelota in mRNA quality control of nonstop mRNA.
  findings:
  - statement: Human Pelota functions in mRNA quality control of nonstop mRNA; the K2A and R45A mutants abolish its ability to rescue stalled ribosomes.
    reference_section_type: RESULTS
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Cached publication title matches; mutational analysis establishes human PELO's stalled-ribosome rescue function in nonstop mRNA QC.
- id: PMID:27863242
  title: Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.
  findings:
  - statement: Cryo-EM of the PELO-HBS1L complex on stalled ribosomes defines PELO's stalled-ribosome sensor activity and ribosome binding.
    reference_section_type: RESULTS
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Cached publication title matches; cryo-EM structural evidence supports the stalled-ribosome sensor activity (GO:0170011 IDA in GOA).
- id: PMID:31515488
  title: Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
  findings: []
- id: PMID:32296183
  title: A reference map of the human binary protein interactome.
  findings: []
- id: PMID:32814053
  title: Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
  findings: []
- id: Reactome:R-HSA-9954730
  title: Reactome ribosome quality control reaction (PELO cytosol)
  findings: []
- id: Reactome:R-HSA-9954919
  title: Reactome ribosome quality control reaction (PELO cytosol)
  findings: []
- id: Reactome:R-HSA-9955731
  title: Reactome ribosome quality control reaction (PELO cytosol)
  findings: []
core_functions:
- description: Stalled-ribosome sensor / eRF1-like factor that recognizes ribosomes stalled at the 3' end of an mRNA by probing the empty mRNA channel and A site, the molecular recognition event that initiates ribosome rescue. Unlike eRF1, PELO lacks peptidyl-tRNA hydrolase activity.
  molecular_function:
    id: GO:0170011
    label: stalled ribosome sensor activity
  locations:
  - id: GO:0022626
    label: cytosolic ribosome
  supported_by:
  - reference_id: file:human/PELO/PELO-uniprot.txt
    supporting_text: PELO recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel
- description: As the eRF1-like subunit of the Pelota-HBS1L (Dom34-Hbs1) complex, with the GTPase HBS1L and recycling ATPase ABCE1, PELO rescues stalled ribosomes by driving their dissociation into subunits, initiating no-go and non-stop mRNA decay.
  molecular_function:
    id: GO:0043022
    label: ribosome binding
  in_complex:
    id: GO:1990533
    label: Dom34-Hbs1 complex
  supported_by:
  - reference_id: PMID:21448132
    supporting_text: Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes
  - reference_id: file:human/PELO/PELO-uniprot.txt
    supporting_text: Component of the Pelota-HBS1L complex, also named Dom34-Hbs1 complex, composed of PELO and HBS1L
proposed_new_terms: []
suggested_questions:
- question: How is the choice between productive translation termination (eRF1) and rescue (PELO) made at ribosomes with short or empty mRNA in the channel?
- question: What is the in vivo contribution of the PINK1-regulated PELO recruitment to mitochondrial ribosomes relative to its canonical cytosolic rescue role?
suggested_experiments:
- description: Ribosome profiling and 5'P degradome sequencing in PELO-knockout versus wild-type human cells to quantify accumulation of stalled/truncated mRNAs and define the endogenous no-go/non-stop substrate repertoire.
- description: Reconstituted single-molecule or cryo-EM time-resolved analysis of PELO-HBS1L-ABCE1 splitting kinetics on defined stalled substrates to dissect the mRNA-channel sensing step.