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000283176 0247_ $$2doi$$a10.1016/j.molcel.2025.12.006
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000283176 1001_ $$0P:(DE-2719)9000582$$aHoffmann, Christian$$b0$$eFirst author$$udzne
000283176 245__ $$aMembrane-protein-mediated phase separation orchestrates organelle contact sites.
000283176 260__ $$a[Cambridge, Mass.]$$bCell Press$$c2026
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000283176 520__ $$aMitochondria and the endoplasmic reticulum (ER) contain large areas that are in close proximity. Yet the mechanism of how these inter-organellar adhesions are formed remains elusive. Tight functional connections, termed 'membrane contact sites,' assemble at these areas and are essential for exchanging metabolites and lipids between the organelles. Recently, the ER-resident protein PDZ domain-containing protein 8 (PDZD8) was identified as a tether between the ER and mitochondria or late endosomes/lysosomes. Here, we show that PDZD8 can undergo phase separation via its intrinsically disordered region (IDR). Endogenously labeled PDZD8 forms condensates on membranes both in vitro and in mammalian cells. Electron microscopy analyses indicate that the expression of full-length PDZD8 rescues the decrease in inter-organelle contacts in PDZD8 knockout cells but not PDZD8 lacking its IDR. Together, this study identifies that PDZD8 condensates at the lipid interfaces act as an adhesive framework that stitches together the neighboring organelles and supports the structural and functional integrity of inter-organelle communication.
000283176 536__ $$0G:(DE-HGF)POF4-351$$a351 - Brain Function (POF4-351)$$cPOF4-351$$fPOF IV$$x0
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000283176 650_7 $$2Other$$aPDZD8
000283176 650_7 $$2Other$$abiomolecular condensates
000283176 650_7 $$2Other$$aendoplasmic reticulum
000283176 650_7 $$2Other$$aliquid-liquid phase separation
000283176 650_7 $$2Other$$amembrane contact sites
000283176 650_7 $$2Other$$amitochondria
000283176 650_7 $$2NLM Chemicals$$aMembrane Proteins
000283176 650_7 $$2NLM Chemicals$$aIntrinsically Disordered Proteins
000283176 650_2 $$2MeSH$$aHumans
000283176 650_2 $$2MeSH$$aEndoplasmic Reticulum: metabolism
000283176 650_2 $$2MeSH$$aEndoplasmic Reticulum: ultrastructure
000283176 650_2 $$2MeSH$$aEndoplasmic Reticulum: genetics
000283176 650_2 $$2MeSH$$aMitochondria: metabolism
000283176 650_2 $$2MeSH$$aMitochondria: ultrastructure
000283176 650_2 $$2MeSH$$aMitochondria: genetics
000283176 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000283176 650_2 $$2MeSH$$aMembrane Proteins: genetics
000283176 650_2 $$2MeSH$$aMembrane Proteins: chemistry
000283176 650_2 $$2MeSH$$aHeLa Cells
000283176 650_2 $$2MeSH$$aHEK293 Cells
000283176 650_2 $$2MeSH$$aAnimals
000283176 650_2 $$2MeSH$$aIntrinsically Disordered Proteins: metabolism
000283176 650_2 $$2MeSH$$aIntrinsically Disordered Proteins: genetics
000283176 650_2 $$2MeSH$$aBiomolecular Condensates: metabolism
000283176 650_2 $$2MeSH$$aPhase Separation
000283176 7001_ $$aNagao, Takahiro$$b1
000283176 7001_ $$aTsunoyama, Taka A$$b2
000283176 7001_ $$0P:(DE-2719)9002092$$aTromm, Johannes Vincent$$b3$$udzne
000283176 7001_ $$0P:(DE-2719)9001041$$aLogan, Chinyere$$b4
000283176 7001_ $$aNakamura, Koki$$b5
000283176 7001_ $$0P:(DE-2719)9001572$$aWang, Han$$b6$$udzne
000283176 7001_ $$aBianchi, Frans$$b7
000283176 7001_ $$avan den Bogaart, Geert$$b8
000283176 7001_ $$aKusumi, Akihiro$$b9
000283176 7001_ $$aHirabayashi, Yusuke$$b10
000283176 7001_ $$0P:(DE-2719)9000670$$aMilovanovic, Dragomir$$b11$$eLast author$$udzne
000283176 773__ $$0PERI:(DE-600)2001948-8$$a10.1016/j.molcel.2025.12.006$$gVol. 86, no. 1, p. 135 - 149.e9$$n1$$p135 - 149.e9$$tMolecular cell$$v86$$x1097-2765$$y2026
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