| Literature DB >> 21618825 |
Hsi-Hsien Lin1, Martin Stacey, Simon Yona, Gin-Wen Chang.
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 recentyears, the conserved cleavage site, molecularmechanism 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.Mesh：
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Year: 2010 PMID： 21618825 DOI： 10.1007/978-1-4419-7913-1_4
Source DB: PubMed Journal: Adv Exp Med Biol ISSN： 0065-2598 Impact factor: 2.622