Proteomics

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Human TRIM72 localizes on the microsome

ABSTRACT: Membrane repair machinery is a unique process to maintain cell integrity. In the early step of repair process, TRIM72 facilitates the patch membranes to damaged sites for resealing membrane and protects cells from acute membrane injury. The TRIM72 is an E3 ubiquitin ligase belonging to tripartite motif (TRIM) superfamily. Not only the repair machinery, the TRIM72 is also known as targeting membrane proteins such as insulin substrate receptor-1 (IRS-1) and insulin receptor (IR), so membrane binding events would be essential for TRIM72 to play a role. We found that the human TRIM72 localizes on the microsomal vesicles with very strong affinity. By the mass spectrometric gene ontology analysis, it has been confirmed the microsomal fractions were originated from the junctional and the exocytic vesicles. Moreover, identified proteins are classified to the cell adhesion and cell adhesion molecule binding. These results suggest that the cellular activity of TRIM72 would be related to vesicular proteins which engage to cell adhesion and furthermore, it should be mediated after membrane trans-localization of TRIM72.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Sehwan Jang  

LAB HEAD: Hyun Kyu Song

PROVIDER: PXD024978 | Pride | 2024-01-26

REPOSITORIES: Pride

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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]

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