Abstract
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.
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Lin, HH., Stacey, M., Yona, S., Chang, GW. (2010). GPS Proteolytic Cleavage of Adhesion-GPCRs. In: Yona, S., Stacey, M. (eds) Adhesion-GPCRs. Advances in Experimental Medicine and Biology, vol 706. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7913-1_4
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DOI: https://doi.org/10.1007/978-1-4419-7913-1_4
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