Nidhi Juneja
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Nidhi Juneja has a total of 23 co-authors. Here are the top co-authors by number of shared publications:
- Albert Koulman
Metabolic Research Laboratories, Institute of Metabolic Science, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK
1 shared publication Andrew M. James
MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK
1 shared publication- Benjamin Jenkins
Metabolic Research Laboratories, Institute of Metabolic Science, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK
1 shared publication - Chak Shun Yu
MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK
1 shared publication Clarissa D. Booth
Center for Genetics and Rare Diseases, Sanford Research, Sioux Falls, USA
1 shared publicationDenis Lacabanne
MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge, UK
1 shared publication
Latest Publications
- Open Access
- 15 September 2026
- Published by Springer Nature in Nature Cell Biology
- Vol. 28 (10) , 2068-2077
The Batten disease protein CLN8 is a stereospecific acyltransferase in bis(monoacylglycero)phosphate biosynthesis
Loss-of-function mutations in the endoplasmic reticulum membrane protein CLN8 cause Batten disease, a neurodegenerative lysosomal storage disorder. CLN8 acts with the lysosomal enzyme CLN5 to produce bis(monoacylglycero)phosphate (BMP), a signature lysosomal phospholipid with unique S , S stereochemistry. However, the role of CLN8 in this pathway has remained unclear. Here we establish that CLN8 is a glycerophosphoglycerol acyltransferase that catalyses the stereospecific acylation of S , S -glycerophosphoglycerol to generate S , S -lysophosphatidylglycerol, the CLN5 substrate in BMP synthesis. Cryo-electron microscopy structures define the CLN8 active site and support a ping-pong acyl transfer mechanism. Batten disease mutations impair CLN8 enzymatic activity and abolish BMP production in mice. Exogenous S , S -lysophosphatidylglycerol, but not the R , S stereoisomer, restores BMP synthesis in CLN8-deficient cells and mice and improves neurological phenotypes in cln8 mutant zebrafish. These findings define the function of CLN8, explain the biochemical basis of CLN8 Batten disease and establish BMP precursor supplementation as a proof-of-concept therapeutic strategy.
- 15 September 2026
- Published by Springer Nature in Nature Cell Biology
- Vol. 28 (10) , 2068-2077
Open AccessThe Batten disease protein CLN8 is a stereospecific acyltransferase in bis(monoacylglycero)phosphate biosynthesis
Loss-of-function mutations in the endoplasmic reticulum membrane protein CLN8 cause Batten disease, a neurodegenerative lysosomal storage disorder. CLN8 acts with the lysosomal enzyme CLN5 to produce bis(monoacylglycero)phosphate (BMP), a signature lysosomal phospholipid with unique S , S stereochemistry. However, the role of CLN8 in this pathway has remained unclear. Here we establish that CLN8 is a glycerophosphoglycerol acyltransferase that catalyses the stereospecific acylation of S , S -glycerophosphoglycerol to generate S , S -lysophosphatidylglycerol, the CLN5 substrate in BMP synthesis. Cryo-electron microscopy structures define the CLN8 active site and support a ping-pong acyl transfer mechanism. Batten disease mutations impair CLN8 enzymatic activity and abolish BMP production in mice. Exogenous S , S -lysophosphatidylglycerol, but not the R , S stereoisomer, restores BMP synthesis in CLN8-deficient cells and mice and improves neurological phenotypes in cln8 mutant zebrafish. These findings define the function of CLN8, explain the biochemical basis of CLN8 Batten disease and establish BMP precursor supplementation as a proof-of-concept therapeutic strategy.