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Updated: Jun 1, 2026

Imaging Molecular Adhesion in Cell Rolling by Adhesion Footprint Assay
Published on: September 27, 2021
GPS proteolytic cleavage of adhesion-GPCRs
Hsi-Hsien Lin1, Martin Stacey, Simon Yona
1Department of Microbiology and Immunology, College of Medicine, Chang Gung University, 259 Wen-Hwa Ist Road, Kwei-San, Tao-Yuan, Taiwan. hhlin@mail.cgu.edu.tw
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.
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