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Now let me review the specific GO-CAM model in question:

GO-CAM Model Review: gomodel:613aae0000000885

Summary

This model titled "SP-ANN-PTPRM" describes interactions between PTPRM (receptor-type tyrosine-protein phosphatase mu), CTNND1 (p120 catenin), ZDHHC7 (palmitoyltransferase), and SLC2A4 (GLUT4) in human cells (NCBITaxon:9606).

Model Components

  1. PTPRM (UniProtKB:P28827) with phosphatase activity at cell-cell junction
  2. CTNND1 (UniProtKB:O60716) with cadherin binding and protein sequestering activities
  3. ZDHHC7 (UniProtKB:Q9NXF8) with palmitoyltransferase activity
  4. SLC2A4/GLUT4 (UniProtKB:P14672) with glucose transmembrane transporter activity

Causal Relationships

  • PTPRM phosphatase activity inhibits CTNND1's sequestering activity
  • CTNND1 cadherin binding leads to CTNND1's protein sequestering activity
  • CTNND1 protein sequestering activity inhibits SLC2A4/GLUT4 transporter activity
  • ZDHHC7 palmitoyltransferase activity activates SLC2A4/GLUT4 transporter activity

Evidence Assessment

The literature evidence supports the model:

  1. PTPRM dephosphorylates p120 catenin (CTNND1), preventing its cytoplasmic localization (PMID:21998202)
  2. CTNND1 binds to cadherins at cell-cell junctions (PMID:15240885, PMID:17047063)
  3. Cytoplasmic CTNND1 can sequester GLUT4 and prevent its localization to the plasma membrane (PMID:21998202)
  4. ZDHHC7 palmitoylates GLUT4/SLC2A4 and regulates its membrane translocation (PMID:28057756)

Strengths

  • The model accurately represents the molecular interactions and causal relationships described in the literature
  • Cellular locations are properly specified (cell surface, cytoplasm, plasma membrane)
  • The use of "protein sequestering activity" (GO:0140311) for CTNND1 is appropriate per GO-CAM guidelines
  • The literature evidence is sufficient and relevant to support all connections

Issues and Recommendations

  1. No issues found: The model follows GO-CAM best practices for representing complexes and protein sequestering activities.

  2. Biological accuracy: The model is consistent with our understanding of how PTPRM regulates adipogenic differentiation via modulation of p120 catenin phosphorylation, which in turn affects GLUT4 trafficking to the plasma membrane.

Conclusion

This GO-CAM model accurately represents the regulatory pathway where PTPRM dephosphorylates p120 catenin (CTNND1), preventing CTNND1-mediated sequestering of GLUT4/SLC2A4, while ZDHHC7 palmitoylates GLUT4 to promote its membrane translocation. The model is well-supported by literature evidence and follows GO-CAM best practices. No corrections are needed.