GPS Proteolytic Cleavage of Adhesion-GPCRs

  • Hsi-Hsien Lin
  • Martin Stacey
  • Simon Yona
  • Gin-Wen Chang
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 706)


The stability and functional diversity of proteins can be greatly modulated by posttranslational modification. Proteolytic cleavage at the GPCR proteolysis site (GPS) has been identified as an intrinsic protein modification process of many adhesion-GPCRs. In recent years, the conserved cleavage site, molecular mechanism and the potential functional implication of the GPS proteolysis have been gradually unveiled. However, many aspects of this unique cleavage reaction including its regulation, the relationship between the cleaved fragments and the functional pathways mediated by the cleaved receptor subunits, remain unanswered. Further investigation of the GPS proteolytic modification shall shed light on the biology of the adhesion-GPCRs.


Autosomal Dominant Polycystic Kidney Disease Polycystic Kidney Disease Pkd1 Gene Tumor Endothelial Marker Adhesion GPCRs 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Landes Bioscience and Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • Hsi-Hsien Lin
    • 1
  • Martin Stacey
  • Simon Yona
  • Gin-Wen Chang
  1. 1.Department of Microbiology and Immunology, College of MedicineChang Gung UniversityKwei-SanTaiwan

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