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

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 the TUG (UBXN9, Aspscr1) protein, a central regulator of GLUT4 trafficking, localizes to the ERGIC, and its deletion enhances anterograde secretory flux, 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 CFTR, a model protein that undergoes unconventional secretion. We conclude that TUG organizes and stabilizes ERGIC membranes to support their roles in diverse cellular membrane trafficking pathways.

INSTRUMENT(S): timsTOF Pro 2

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Embryonic Fibroblast

SUBMITTER: Guillaume CHEVREUX

LAB HEAD: Ishier RAOTE

PROVIDER: PXD064240 | Pride | 2025-06-10

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	2431005_Lysate-MEF_Ttest-WT-vs-KO.xlsx	Xlsx
	2431005_Lysate.sne	Other
	2431005_Lysate_KO_1_S4-C10_1_14093.d.zip	Other
	2431005_Lysate_KO_2_S4-C11_1_14094.d.zip	Other
	2431005_Lysate_KO_3_S4-C12_1_14095.d.zip	Other

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

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