TUG protein acts through a disordered region to organize the early secretory pathway

Anup Parchure (), Helen Tejada, Zhiqun Xi, Yeongho Kim, Maohan Su, You Yan, Omar Julca-Zevallos, Abel R. Alcázar-Román, Marie Villemeur, Xinran Liu, Derek Toomre, Ishier Raote and Jonathan S. Bogan ()
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Anup Parchure: Yale School of Medicine
Helen Tejada: Yale School of Medicine
Zhiqun Xi: Yale School of Medicine
Yeongho Kim: Yale School of Medicine
Maohan Su: Yale School of Medicine
Omar Julca-Zevallos: Yale School of Medicine
Abel R. Alcázar-Román: Yale School of Medicine
Marie Villemeur: Institut Jacques Monod
Xinran Liu: Yale School of Medicine
Derek Toomre: Yale School of Medicine
Ishier Raote: Institut Jacques Monod
Jonathan S. Bogan: Yale School of Medicine

Nature Communications, 2025, vol. 16, issue 1, 1-20

Abstract: Abstract The Endoplasmic Reticulum (ER)-Golgi Intermediate Compartment (ERGIC) is a network of tubules and vesicles known for producing COPI vesicles and receiving COPII vesicles from the ER. Much about its identity, stability, and regulation remains unknown. Here, we show that TUG (UBXN9, Aspscr1) protein, a central regulator of GLUT4 trafficking, localizes to the ERGIC, and that its deletion enhances anterograde flux of a model soluble cargo protein. TUG deletion redistributes ERGIC markers to the cis-Golgi and alters Golgi morphology. TUG forms biomolecular condensates in vitro and contains a central disordered region that mediates its recruitment to ERGIC membranes. A distinct N-terminal region mediates its oligomerization in cells. TUG deletion disrupts ERGIC-dependent processes, including autophagy and collagen secretion, and alters the targeting of the CFTR chloride channel. We conclude that TUG organizes and stabilizes ERGIC membranes to support their roles in diverse secretory and degradative membrane trafficking pathways.

Date: 2025
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DOI: 10.1038/s41467-025-60691-8

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