Abstract:
:Proteolytic processing is an important post-translational modification affecting protein activity and stability. In the current study, we investigate the N-terminal cleavage of Trop2, a protein which is overexpressed in many cancers. We demonstrate that Trop2 is cleaved at Arg87 by a transmembrane serine protease, matriptase. Homology modeling and site-directed mutagenesis of amino acids in close proximity to the matriptase cleavage site reveal the importance of Val194 in regulating Trop2 cleavage. Co-immunoprecipitation studies confirm that amino acid substitutions at Arg87, Thr88, Lys189, Val194, and His195 do not affect Trop2 dimerization. However, cleavage of wild-type Trop2 by matriptase is inhibited when it is allowed to dimerize with a V194 A mutant monomer, further confirming the role of Val194 in matriptase-mediated N-terminal cleavage.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kamble PR,Rane S,Breed AA,Joseph S,Mahale SD,Pathak BRdoi
10.1002/1873-3468.13899subject
Has Abstractpub_date
2020-10-01 00:00:00pages
3156-3169issue
19eissn
0014-5793issn
1873-3468journal_volume
594pub_type
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