TRIM72 cross-linked by the higher-order assembly on the negatively charged liposome surface

ABSTRACT: Plasma membrane repair is a rapid cellular response for resealing of membrane for cell survival. In the early step of repair process, TRIM72 is known to a key initiator for facilitating patch membrane to the damaged membrane site. When acute membrane injury happens, TRIM72 is also known to sensitively generate disulfide bonds formations by reactive oxygen species and further oligomerize with each other. We tried to clarify this repair system using in vitro reconstruction of TRIM72-liposome complex and find critical sites using cross-linker mass spectrometry. Using each four different length of sulfhydryl reactive cross-linkers, TRIM72 cross-linked with each other on the negatively charged liposome surface only. We also identified that the cross-linking bridges were highly conserved except bismaleimidoethane as a shortest arm length about 8 Å only. Our results indicated that the B2-box/B2-box locates closely with each other on the liposome surface. Furthermore, freely open RING domain is rearranged into the specific conformation, where located near the H2 helix of coiled coil domain. It suggests that the conformational changes of TRIM72 are induced by higher order assembly on the negative charged membrane surface.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Sehwan Jang  

LAB HEAD: Hyun Kyu Song

PROVIDER: PXD024946 | Pride | 2024-01-26

REPOSITORIES: Pride