GPS proteolytic cleavage of adhesion-GPCRs

Hsi Hsien Lin*, Martin Stacey, Simon Yona, Gin Wen Chang

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

28 Scopus citations


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.

Original languageEnglish
Title of host publicationAdhesion-GPCRs
Subtitle of host publicationStructure to Function
EditorsSimon Yona, Martin Stacey
Number of pages10
StatePublished - 2010

Publication series

NameAdvances in Experimental Medicine and Biology
ISSN (Print)0065-2598


Dive into the research topics of 'GPS proteolytic cleavage of adhesion-GPCRs'. Together they form a unique fingerprint.

Cite this