Finding. When Chlamydomonas comes off nutrient stress, lipid droplets have to talk to mitochondria and peroxisomes to burn what they stored. Blot, Li-Beisson and colleagues show that Delayed in TAG Hydrolysis 1 (DTH1) is the surface protein that makes that conversation possible. Knock it out and droplet breakdown stalls. Isolated-droplet lipidomics and proteomics say phosphatidylethanolamine is part of the degradation lipid code, the droplet proteome and lipidome fail to remodel, and communication among droplets, peroxisomes, and mitochondria is one of the missing pieces. During nitrogen recovery the cells also make micro-lipid droplets, a structure the authors say has not been reported in microalgae.
Why this paper matters
DTH1 looks like a scaffold: coiled-coil, PE-specific lipid binding, disordered stretches, a helical tail. That is a recruitment and tethering resume. The mitochondrial reason to keep the paper is not a new respiratory-chain subunit. It is carbon trafficking: stored triacylglycerol does not become ATP unless the droplet can hand fatty acids to the other two oxidative organelles. A knockout that breaks that triangle is a contact-site paper even if the abstract never says "contact site."
What they actually measured
Wild-type versus dth1 isolated lipid droplets, lipidome plus proteome, during nutrient recovery, with a closer look at nitrogen. PE as a lipid species tied to degradation. Organelle-communication language from those omics. Micro-LDs as a morphological observation.
How to read the score
Mid 70s. Real mitochondrial involvement, algal, omics-inferred contacts. Confidence is medium for physical tethering.
Caveats
No live mitochondrial-LD contact assay is claimed here. Animal brown-fat or liver LD biology is a different protein cast.
What to do with it
If you map LD-mitochondria-peroxisome triangles, pull the dth1 LD proteome and the PE lipidome. If you work on mammalian seipin or perilipin contacts, treat this as a green-lineage analogue, not a homolog claim.