Dataset Information

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): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Sehwan Jang

LAB HEAD: Hyun Kyu Song

PROVIDER: PXD024946 | Pride | 2024-01-26

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	210201_KOREA_crosslink_gel1_NCE25.raw	Raw
	210201_KOREA_crosslink_gel1_NCE25_HCDFT.pf2	Other
	210201_KOREA_crosslink_gel5_NCE25.raw	Raw
	210201_KOREA_crosslink_gel5_NCE25_HCDFT.pf2	Other
	210201_KOREA_crosslink_gel7_NCE25.raw	Raw

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Publications

Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane.

Park Si Hoon SH Han Juhyun J Jeong Byung-Cheon BC Song Ju Han JH Jang Se Hwan SH Jeong Hyeongseop H Kim Bong Heon BH Ko Young-Gyu YG Park Zee-Yong ZY Lee Kyung Eun KE Hyun Jaekyung J Song Hyun Kyu HK

Nature structural & molecular biology 20230928 11

Defects in plasma membrane repair can lead to muscle and heart diseases in humans. Tripartite motif-containing protein (TRIM)72 (mitsugumin 53; MG53) has been determined to rapidly nucleate vesicles at the site of membrane damage, but the underlying molecular mechanisms remain poorly understood. Here we present the structure of Mus musculus TRIM72, a complete model of a TRIM E3 ubiquitin ligase. We demonstrated that the interaction between TRIM72 and phosphatidylserine-enriched membranes is nece ...[more]

PMID: 37770719

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