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Related Concept Videos

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...

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Related Experiment Video

Updated: Jul 1, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Manipulating PTPRD function with ectodomain antibodies.

Zhe Qian1,2, Dongyan Song1, Jonathan J Ipsaro3

  • 1Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA.

Genes & Development
|September 5, 2023
PubMed
Summary
This summary is machine-generated.

Antibodies targeting Receptor Protein Tyrosine Phosphatase Delta (RPTPδ/PTPRD) inhibit its activity and promote degradation, suppressing tumor-promoting signaling and cell invasion.

Keywords:
PTPRDSRCbivalent antibodydimerizationprotein tyrosine phosphorylationreceptor protein tyrosine phosphatase

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Area of Science:

  • Molecular Biology
  • Cancer Research
  • Drug Development

Background:

  • Protein tyrosine phosphatases (PTPs) regulate signal transduction but are underexplored drug targets.
  • Receptor protein tyrosine phosphatase delta (RPTPδ/PTPRD) promotes tumor progression and metastasis by increasing SRC activity.
  • Receptor protein tyrosine phosphatases (RPTPs) inhibition is linked to dimerization.

Purpose of the Study:

  • To develop antibodies targeting extracellular domains of RPTPδ/PTPRD to modulate dimerization and signaling.
  • To investigate the therapeutic potential of targeting RPTPδ/PTPRD in cancer.

Main Methods:

  • Generation of antibodies against PTPRD ectodomains.
  • Validation of antibody binding to endogenous PTPRD in metastatic breast cancer cells (CAL51).
  • Assessment of antibody-induced changes in phosphatase activity, dimerization, and degradation pathways (lysosomal and proteasomal).

Main Results:

  • Monoclonal antibody RD-43 bound endogenous PTPRD, inhibited its phosphatase activity, and induced PTPRD degradation.
  • RD-43 triggered PTPRD dimerization, impairing catalytic activity.
  • Antibody-mediated PTPRD degradation occurred via lysosomal and proteasomal pathways, independent of secretase cleavage.
  • RD-43 treatment inhibited SRC signaling and PTPRD-dependent cell invasion.

Conclusions:

  • Targeting extracellular RPTPδ/PTPRD with antibodies can inhibit its tumor-promoting functions.
  • Antibody-induced dimerization and subsequent degradation of RPTPδ/PTPRD represent a viable therapeutic strategy.
  • This approach holds therapeutic potential for cancers driven by RPTPδ/PTPRD.