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Label-free proteomics of immuno-purified SYP61-trans-Golgi Network compartment in control condition and upon sphingolipid acyl-chain length reduction by metazachlor.

ABSTRACT: The trans-Golgi Network (TGN) in plants is a main sorting hub for proteins and lipids. The lipid composition at the TGN is instrumental to the polar sorting of the auxin efflux carrier PIN2 from TGN to the apical membrane. Here, we immuno-purified the full and intact TGN using the TGN-resident syntaxin SYP61 to identify and quantify TGN-proteins which abundance at TGN is dependent on the acyl-chain length of very-long chain fatty acids-containing lipids such as sphingolipids.

INSTRUMENT(S): Q Exactive

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

SUBMITTER: Stephane Claverol

LAB HEAD: Bonneu M

PROVIDER: PXD026252 | Pride | 2021-12-01

REPOSITORIES: Pride

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			Action	DRS
	Table.xlsx	Xlsx
	checksum.txt	Txt
	yb160915_09b.raw	Raw
	yb160915_09b_NG.xlsx	Xlsx
	yb160915_10.raw	Raw

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