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biorxiv2026-09-06cancerproteostasisone-carbontranslation

Mitochondrial HSP60 (HSPD1) holds MYCN up in amplified neuroblastoma

Deplete HSPD1 (HSP60) in MYCN-amplified neuroblastoma and mitochondrial translation falls, MYCN itself falls, and tumors shrink in vitro and in vivo. HSPD1 RNA and protein track MYCN in tumors. The chaperone is not just a MYCN slave.

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Signal profile (abstract-level)

cancer · proteostasis · one-carbon · translation

Score 85/100BIORXIVhigh confidencecancer
85
Importance
50
Mito signal
67
Dysfunction
75
Evidence
73
Translational

Editorial signal profile from the abstract (importance score, mito keywords, dysfunction tags, evidence density, translational cues). Not a figure reproduced from the preprint PDF.

Finding. MYCN-amplified neuroblastoma lives on a mitochondrial proteome the transcription factor ordered. Alassam, Rotblat and colleagues take the chaperone HSPD1 (mitochondrial HSP60) away. Mitochondrial translation falls. MYCN itself falls. Tumors fail in culture and in mice. In patient tumors, HSPD1 travels with MYCN. The chaperone that folds MTHFD2 and keeps mitoribosomal proteins soluble is also holding the oncogene up.

Score 85. Feedback onto MYCN, in-vivo, tumor correlation, named clients.

What to do with it Put HSPD1 above MYCN as well as below. Check whether MTHFD2 loss copies the MYCN drop.

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Source preprint

HSPD1 promotes neuroblastoma by augmenting MYCN expression

10.64898/2026.09.03.749066

Alassam SS, Manikandan DB, Ben-David H, Cohen L, Kaluski-Kopatch S, Hruby L, Dror S, Sorensen P, Delaidelli A, Leprivier G, Elkabets M, Rotblat B.

Open on biorxiv →PDF

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