Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation

Yong Mi Choi, Dalila Ajjaji, Kaelin D. Fleming, Peter P. Borbat, Meredith L. Jenkins, Brandon E. Moeller, Shaveen Fernando, Surita R. Bhatia, Jack H. Freed, John E. Burke (), Abdou Rachid Thiam () and Michael V. Airola ()
Additional contact information
Yong Mi Choi: Stony Brook University
Dalila Ajjaji: ENS, Université PSL, CNRS, Sorbonne Université, Université Paris Cité
Kaelin D. Fleming: University of Victoria
Peter P. Borbat: Cornell University
Meredith L. Jenkins: University of Victoria
Brandon E. Moeller: University of Victoria
Shaveen Fernando: Stony Brook University
Surita R. Bhatia: Stony Brook University
Jack H. Freed: Cornell University
John E. Burke: University of Victoria
Abdou Rachid Thiam: ENS, Université PSL, CNRS, Sorbonne Université, Université Paris Cité
Michael V. Airola: Stony Brook University

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract Lipid droplets (LDs) are dynamic organelles that contain an oil core mainly composed of triglycerides (TAG) that is surrounded by a phospholipid monolayer and LD-associated proteins called perilipins (PLINs). During LD biogenesis, perilipin 3 (PLIN3) is recruited to nascent LDs as they emerge from the endoplasmic reticulum. Here, we analyze how lipid composition affects PLIN3 recruitment to membrane bilayers and LDs, and the structural changes that occur upon membrane binding. We find that the TAG precursors phosphatidic acid and diacylglycerol (DAG) recruit PLIN3 to membrane bilayers and define an expanded Perilipin-ADRP-Tip47 (PAT) domain that preferentially binds DAG-enriched membranes. Membrane binding induces a disorder to order transition of alpha helices within the PAT domain and 11-mer repeats, with intramolecular distance measurements consistent with the expanded PAT domain adopting a folded but dynamic structure upon membrane binding. In cells, PLIN3 is recruited to DAG-enriched ER membranes, and this requires both the PAT domain and 11-mer repeats. This provides molecular details of PLIN3 recruitment to nascent LDs and identifies a function of the PAT domain of PLIN3 in DAG binding.

Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-023-38725-w Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38725-w

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-023-38725-w

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().