ArticleProtoplasma2026
Integrative phosphoproteomic network analysis identifies CAMK2D as a shared regulator of TPD52 family proteins in cancer.
Article in Protoplasma, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
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.
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Who cites it
3 citing papers in PubMed.
- Co-Phosphoregulatory Network Underlying Functional Coherence of TLK1 and TLK2 Kinase Paralogs.International journal of molecular sciences · 2026Article
- Phosphosite-specific co-regulation networks of MELK kinase: insights from integrative global phosphoproteomes.Journal, genetic engineering & biotechnology · 2026Article
- Multifaceted roles of fibronectin type III domain containing 3B (FNDC3B) in cell biology and signaling.Frontiers in molecular biosciences · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Tumour Protein D52 (TPD52) family, including TPD52, TPD52L1, and TPD52L2, plays critical roles in membrane trafficking, lipid metabolism, and oncogenic signalling, with its overexpression linked to multiple cancers. Phosphorylation is a key regulator of their functions, yet their phosphoproteomic landscape remains underexplored. This study integrates over 3,825 public human phosphoproteomic datasets to map phosphorylation profiles of TPD52, TPD52L1, and TPD52L2, identifying dominant phosphosites like S171, S176, S149, and S12, S166 within conserved coiled-coil and PEST-like domains. CAMK2D was identified as a predominant shared kinase, alongside CDK2 and GRK5, associating these modifications with calcium signaling, cell cycle progression, and cytoskeletal remodeling. Co-phosphoregulation highlighted positive interactions with ABRAXAS2 and negative correlations with ABLIM3, implicating involvement in ubiquitin-mediated degradation, epithelial-mesenchymal transition (EMT), and cytokinesis. Notably, hypophosphorylation at TPD52_S171/S176 was observed in hepatocellular and lung carcinomas, whereas hyperphosphorylation at TPD52L2_S166 prevailed in ovarian and pancreatic cancers, underscoring biomarker utility. Phosphorylation-driven interactomes emphasized roles in vesicular trafficking and oncogenesis This study catalogues the phosphorylation events and explores the potential of TPD52 family as a phosphoregulated hub in cancer biology, with CAMK2D as a potential therapeutic target.
Indexed as
Identifiers
41364128What Socratic holds
Registered trials
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 Socratic graph.