Dataset Information

Proximity labeling – LC/MS-MS with ERC1-TurboID/atg7-2 Arabidopsis seedlings

ABSTRACT: Given that ERC1 proteins are enriched on membraneless condensates together with ATG8 proteins prior to autophagosome formation, we hypothesized that ERC1-positive condensates might serve as an assembly site for ATG8 proteins and other adaptors before ATG8 proteins are conjugated onto the phagophore membrane. In order to identify other possible components related to the ERC1 condensates, we generated transgenic plants expressing TurboID-tagged ERC1 in the atg7-2 background. TurboID-coupled mass spectrometry revealed that, in addition to ATG8e, the selective autophagy receptor NBR1 was also significantly enriched.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Seedling

SUBMITTER: Shouling Xu

LAB HEAD: Shouling Xu

PROVIDER: PXD067354 | Pride | 2025-10-07

REPOSITORIES: Pride

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Publications

Biomolecular condensation of ERC1 recruits ATG8 and NBR1 to drive autophagosome formation for plant heat tolerance.

Chung Ka Kit KK Zhao Ziwei Z Law Kai Ching KC Ma Juncai J Chiang Cheuk Him CH Leung Kwan Ho KH Shrestha Ruben R Wu Yixin Y Li Chaorui C Lee Ka Ming KM Feng Lei L Li Xibao X Wong Kam Bo KB Xu Shou-Ling SL Gao Caiji C Zhuang Xiaohong X

bioRxiv : the preprint server for biology 20240910

Macroautophagy (hereafter autophagy) is essential for cells to respond to nutrient stress by delivering cytosolic contents to vacuoles for degradation via the formation of a multi-layer vesicle named autophagosome. A set of autophagy-related (ATG) regulators are recruited to the phagophore assembly site for the initiation of phagophore, as well as its expansion and closure and subsequent delivery into the vacuole. However, it remains elusive that how the phagophore assembly is regulated under di ...[more]

PMID: 39314317

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			Action	DRS
	ERC1_TurboID_1.raw	Raw
	ERC1_TurboID_2.raw	Raw
	ERC1_TurboID_3.raw	Raw
	TurboID_Control_1.raw	Raw
	TurboID_Control_2.raw	Raw