Evidence map›Paper›PMID 38859931›Full record

ReviewFrontiers in molecular biosciences2024

Cleavage of Hsp70.1 causes lysosomal cell death under stress conditions.

Tetsumori Yamashima, Daria Mochly-Rosen, Soichi Wakatsuki, Eishiro Mizukoshi, Takuya Seike, Isabel Maria Larus, Che-Hong Chen, Miho Takemura, Hisashi Saito, Akihiro Ohashi

Abstract readReview
In one paragraph

Review in Frontiers in molecular biosciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. A window into intracellular events in myositis through subcellular proteomics.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025
    Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Bacteria in hypertrophic scars promote scar formation through HSBP1-mediated autophagy.Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society
    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

10 authors.

Tetsumori YamashimaDepartment of Psychiatry and Behavioral Science, Kanazawa University Graduate School of Medical Sciences, Kanazawa, Japan.
Daria Mochly-RosenDepartment of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, United States.
Soichi WakatsukiDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, United States.
Eishiro MizukoshiDepartment of Gastroenterology, Kanazawa University Graduate School of Medical Sciences, Kanazawa, Japan.
Takuya SeikeDepartment of Gastroenterology, Kanazawa University Graduate School of Medical Sciences, Kanazawa, Japan.
Isabel Maria LarusDepartment of Structural Biology, Stanford University School of Medicine, Stanford, CA, United States.
Che-Hong ChenDepartment of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA, United States.
Miho TakemuraLaboratory of Gene Function, Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Japan.
Hisashi SaitoDivision of Collaborative Research and Development, Exploratory Oncology Research and Clinical Trial Center, National Cancer Center, Kashiwa, Japan.
Akihiro OhashiDivision of Collaborative Research and Development, Exploratory Oncology Research and Clinical Trial Center, National Cancer Center, Kashiwa, Japan.

Funding

Stanford ChEM-H Chemistry/Biology Interface Predoctoral Training ProgramT32GM139791 · NIGMS · STANFORD UNIVERSITY · PI Carolyn Bertozzi, Christine Jacobs-Wagner · 2021 to 2026
$2.4M
NIGMS NIH HHS T32 GM139791
6 · The paper itself

Abstract

Autophagy mediates the degradation of intracellular macromolecules and organelles within lysosomes. There are three types of autophagy: macroautophagy, microautophagy, and chaperone-mediated autophagy. Heat shock protein 70.1 (Hsp70.1) exhibits dual functions as a chaperone protein and a lysosomal membrane stabilizer. Since chaperone-mediated autophagy participates in the recycling of ∼30% cytosolic proteins, its disorder causes cell susceptibility to stress conditions. Cargo proteins destined for degradation such as amyloid precursor protein and tau protein are trafficked by Hsp70.1 from the cytosol into lysosomes. Hsp70.1 is composed of an N-terminal nucleotide-binding domain (NBD) and a C-terminal domain that binds to cargo proteins, termed the substrate-binding domain (SBD). The NBD and SBD are connected by the interdomain linker L

Indexed as

ALDH2calpain–cathepsin hypothesischaperone-mediated autophagyHsp70.1hydroxynonenalLAMP2Alifestyle-related diseaselysosomal cell death

Identifiers

PMID38859931
PMCPMC11163108

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.