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Updated: Jan 9, 2026

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

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Integrative phosphoproteomic network analysis identifies CAMK2D as a shared regulator of TPD52 family proteins in

Noreen A Khan1, Amal Fahma1, Althaf Mahin1

  • 1Centre for Integrative Omics Data Science, Yenepoya (Deemed to be University), Mangalore, 575018, Karnataka, India.

Protoplasma
|December 9, 2025
PubMed

Insights

This study maps phosphorylation sites on the Tumour Protein D52 (TPD52) family, revealing kinase interactions and altered phosphorylation patterns in various cancers. These findings highlight TPD52 family proteins as potential cancer biomarkers and therapeutic targets.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Proteomics

Background:

  • The Tumour Protein D52 (TPD52) family (TPD52, TPD52L1, TPD52L2) is implicated in membrane trafficking, lipid metabolism, and cancer signaling.
  • Overexpression of TPD52 family members is linked to various cancers.
  • The role of phosphorylation in TPD52 family function is not well understood, despite its importance as a regulatory mechanism.

Purpose of the Study:

  • To comprehensively map the phosphoproteomic landscape of the TPD52 family.
  • To identify key kinases and interacting proteins involved in TPD52 family phosphorylation.
  • To investigate the potential of TPD52 family phosphorylation patterns as cancer biomarkers.

Main Methods:

  • Integration of over 3,825 public human phosphoproteomic datasets.
  • Identification and analysis of dominant phosphosites within conserved domains.
  • Kinase-substrate prediction and co-phosphoregulation network analysis.

Main Results:

  • Dominant phosphosites (e.g., S171, S176, S149, S12, S166) were identified in TPD52, TPD52L1, and TPD52L2.
  • CAMK2D, CDK2, and GRK5 were identified as predominant kinases, linking phosphorylation to calcium signaling, cell cycle, and cytoskeleton.
  • Altered phosphorylation patterns (hypo- and hyperphosphorylation) were observed in specific cancer types (e.g., hepatocellular, lung, ovarian, pancreatic cancers).

Conclusions:

  • This study provides a detailed catalogue of TPD52 family phosphorylation events.
  • TPD52 family proteins function as a phosphoregulated hub in cancer biology, influencing processes like EMT and cytokinesis.
  • Specific phosphorylation sites and kinases, such as CAMK2D, represent potential diagnostic biomarkers and therapeutic targets in cancer.
Keywords:
TPD52 CAMK2DKinase cancerPhosphoproteomics

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