MMP7 cleavage of amino-terminal CD95 death receptor switches signaling toward non-apoptotic pathways.

ABSTRACT: CD95 is a death receptor that can promote oncogenesis through molecular mechanisms that are not fully elucidated. Although the mature CD95 membrane receptor is considered to start with the arginine at position 17 after elimination of the signal peptide, this receptor can also be cleaved by MMP7 upstream of its leucine at position 37. This post-translational modification occurs in cancer cells but also in normal cells such as peripheral blood leukocytes. The non-cleaved CD95 amino-terminal region consists in a disordered domain and its in silico reconstitution suggests that it might contribute to receptor aggregation and thereby, regulate the downstream death signaling pathways. In agreement with this molecular modeling analysis, the comparison of CD95-deficient cells reconstituted with ful

SUBMITTER: Kenji SF 

PROVIDER: S-EPMC9588774 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature