Proteomics

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Characterization of m-lipin using HDX-MS

ABSTRACT: This project consists of two experiments. The first is mapping the binding interface between the isolated m-lip domain of mouse lipin and liposomes. The second experiments is mapping the binding interface between full length mouse lipin and liposomes. Looking at the isolated m-lip domain, we found that residues 470-490 and 500-550 showed decreases in exchange upon liposome binding. The full-length lipin experiment saw decreases in exchnage in these same regions, as well as in the very C-terminus and very N-terminus regions of the protein. An order-disorder experiment was done on full length lipin where the protein was exposed to a short pulse of deuterium and compared to the fully-deuterated protein. In this instance, we established that the majority of the protein is relatively disordered and does not have secondary structure with high stability

INSTRUMENT(S): impact HD

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: John Burke  

LAB HEAD: John Burke

PROVIDER: PXD022172 | Pride | 2021-06-29

REPOSITORIES: Pride

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Publications

The middle lipin domain adopts a membrane-binding dimeric protein fold.

Gu Weijing W   Gao Shujuan S   Wang Huan H   Fleming Kaelin D KD   Hoffmann Reece M RM   Yang Jong Won JW   Patel Nimi M NM   Choi Yong Mi YM   Burke John E JE   Reue Karen K   Airola Michael V MV  

Nature communications 20210805 1

Phospholipid synthesis and fat storage as triglycerides are regulated by lipin phosphatidic acid phosphatases (PAPs), whose enzymatic PAP function requires association with cellular membranes. Using hydrogen deuterium exchange mass spectrometry, we find mouse lipin 1 binds membranes through an N-terminal amphipathic helix, the Ig-like domain and HAD phosphatase catalytic core, and a middle lipin (M-Lip) domain that is conserved in mammalian and mammalian-like lipins. Crystal structures of the M-  ...[more]

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