---
title: "ALK endocytosis drives glucose uptake in ALK‑amplified neuroblastoma"
id: "biorxiv-6-endocytosis-of-alk-promotes-glucose-uptake-in-alk-amplified-neuroblastoma"
canonical_url: "https://medichelpline.com/clinical-feed/biorxiv-6-endocytosis-of-alk-promotes-glucose-uptake-in-alk-amplified-neuroblastoma"
content_type: "clinical_feed_article"
specialty: "Oncology"
source_name: "bioRxiv (Biomedical Preprints)"
source_url: "https://www.biorxiv.org/content/10.64898/2026.08.04.742396v1?rss=1"
published_at: "2026-08-05T12:00:00.000Z"
evidence_level: "Verified Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# ALK endocytosis drives glucose uptake in ALK‑amplified neuroblastoma
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/biorxiv-6-endocytosis-of-alk-promotes-glucose-uptake-in-alk-amplified-neuroblastoma
- **Specialty:** [Oncology](https://medichelpline.com/clinical-feed/oncology.md)
- **Primary Source:** bioRxiv (Biomedical Preprints)
- **Source URL:** [Original Journal Publication](https://www.biorxiv.org/content/10.64898/2026.08.04.742396v1?rss=1)
- **Published At:** 2026-08-05T12:00:00.000Z
- **Evidence Rating:** Verified Feed
## Executive GIST (TL;DR)
- The preprint reports that endocytosis of the receptor tyrosine kinase **ALK** promotes cellular **glucose uptake** in neuroblastoma cells with **ALK** amplification. - Using neuroblastoma cell lines with distinct ALK alterations, the authors found that inhibition of ALK activity or receptor endocytosis reduced glucose uptake by approximately **40–50%** in **ALK‑amplified** cells but not in ALK‑mutant cells. - The effect on glucose uptake was independent of the canonical ERK MAPK and PI3K‑AKT signaling pathways. - The glucose uptake mechanism required **dynamin‑dependent endocytosis**, cytoplasmic **dynein**, and the glucose transporter **GLUT1**. - Overexpressed ALK was observed to co‑endocytose with **GLUT1** into vesicles that are transported toward mitochondria, suggesting RTK‑containing endocytic vesicles deliver extracellular glucose to mitochondrial hexokinases. - Inhibition of ALK activity or of endocytosis suppressed glucose uptake but produced no additive inhibition when combined, consistent with a shared pathway. - Disruption of the endocytic machinery selectively impaired growth of **ALK‑amplified** neuroblastoma cells, indicating a potential metabolic vulnerability in RTK‑driven cancers. - This work was posted as a bioRxiv preprint and has not been peer reviewed; funding sources and competing interest disclosures are reported in the source.
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Ryouhei Tsutsumi 1 Kitasato University School of Medicine; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Ryouhei%2BTsutsumi%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Tsutsumi%20R&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3ARyouhei%2BTsutsumi%2B) * [ORCID record for Ryouhei Tsutsumi](http://orcid.org/0000-0002-1704-0362 "Open in new tab") * For correspondence: tsutsumi.ryohei@kitasato-u.ac.jp Shoko Hikage 1 Kitasato University School of Medicine; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Shoko%2BHikage%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Hikage%20S&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AShoko%2BHikage%2B) Shinichi Kiyonari 2 Kitasato University school of Medicine * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Shinichi%2BKiyonari%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Kiyonari%20S&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AShinichi%2BKiyonari%2B) Ryuichi Sakai 1 Kitasato University School of Medicine; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Ryuichi%2BSakai%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Sakai%20R&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3ARyuichi%2BSakai%2B) * [Abstract](https://www.biorxiv.org/content/10.64898/2026.08.04.742396v1)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_art/node:5680449/1) * [Info/History](https://www.biorxiv.org/content/10.64898/2026.08.04.742396v1.article-info)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_info/node:5680449/1) * [Metrics](https://www.biorxiv.org/content/10.64898/2026.08.04.742396v1.article-metrics)[](https://www.biorxiv.org/panels_ajax_tab/article_tab_metrics/node:5680449/1) * [Supplementary material](https://www.biorxiv.org/content/10.64898/2026.08.04.742396v1.supplementary-material)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_data/node:5680449/1) * [ Preview PDF](https://www.biorxiv.org/content/10.64898/2026.08.04.742396v1.full.pdf+html)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_pdf/node:5680449/1) ![Loading](https://www.biorxiv.org/sites/all/modules/contrib/panels_ajax_tab/images/loading.gif) ## Abstract Activated receptor tyrosine kinases (RTKs), such as epidermal growth factor receptor (EGFR) and anaplastic lymphoma kinase (ALK), trigger intracellular signaling while undergoing receptor endocytosis. We recently identified a noncanonical mechanism in which RTK-containing endocytic vesicles deliver extracellular glucose to hexokinases associated with the outer mitochondrial membrane, thereby promoting cellular glucose uptake. Whether this mechanism contributes to cancer metabolism, however, remains unknown. Here, using neuroblastoma cell lines with distinct _ALK_ alterations, we investigated the role of ALK endocytosis in glucose uptake. _ALK_ -amplified, but not _ALK_ -mutant, neuroblastoma cells exhibited a ~40-50% reduction in glucose uptake following inhibition of ALK or receptor endocytosis. This process was independent of the ERK MAPK and PI3K-AKT pathways but required dynamin-dependent endocytosis, cytoplasmic dynein, and GLUT1. Overexpressed ALK constitutively co-endocytosed with GLUT1 into vesicles transported to mitochondria. Inhibition of ALK activity or endocytosis suppressed glucose uptake without producing an additive effect, indicating that both function within the same pathway. Furthermore, disruption of the endocytic machinery selectively impaired the growth of _ALK_ -amplified neuroblastoma cells. These findings identify ALK endocytosis as a major regulator of glucose uptake in _ALK_ -amplified neuroblastoma and suggest that RTK endocytosis represents a previously unrecognized metabolic vulnerability that may be therapeutically exploitable in RTK-driven cancers. ### Competing Interest Statement The authors have declared no competing interest. ## Funder Information Declared Japan Society for the Promotion of Science, 24K10317 Sumitomo Foundation, https://ror.org/01nmpj461 Uehara Memorial Foundation, https://ror.org/00gc20a07 Copyright The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a [CC-BY-NC-ND 4.0 International license](http://creativecommons.org/licenses/by-nc-nd/4.0/). bioRxiv and medRxiv thank the following for their generous financial support: > The Chan Zuckerberg Initiative, Cold Spring Harbor Laboratory, the Sergey Brin Family Foundation, California Institute of Technology, Centre National de la Recherche Scientifique, Fred Hutchinson Cancer Center, Imperial College London, Massachusetts Institute of Technology, Stanford University, The University of Edinburgh, University of Washington, and Vrije Universiteit Amsterdam. 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