Dataset Information

ACBD5 phosphorylationsite analysis

ABSTRACT: Peroxisomes (POs) and the endoplasmic reticulum (ER) cooperate in cellular lipid metabolism and form membrane contacts, which are mediated by the peroxisomal membrane proteins acyl-coenzyme A-binding domain protein 4 and 5 (ACBD4/5) which bind to the resident ER protein vesicle-associated membrane protein-associated protein B (VAPB). ACBD4/5 bind to the major sperm protein (MSP) domain of VAPB via their FFAT-like [two phenylalanines (FF) in an acidic tract] motif. The molecular mechanisms which regulate membrane contact site formation and dynamics are not well explored, in particular in mammalian cells. Here, we reveal that peroxisome-ER associations via the ACBD5-VAPB tether are regulated by phosphorylation.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Fibroblast

SUBMITTER: Friedel Drepper

LAB HEAD: Bettina Warscheid

PROVIDER: PXD018005 | Pride | 2022-01-10

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	3b8384316893a8d4___QEplus022903.mgf.export.F002273.dat	Mgf
	3b8384316893a8d4___QEplus022920.mgf.export.F002272.dat	Mgf
	3b8384316893a8d4___QEplus023588.mgf.export.F002270.dat	Mgf
	3b8384316893a8d4___QEplus023611.mgf.export.F002274.dat	Mgf
	QEplus022902.dat	Other

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Publications

Regulating peroxisome-ER contacts via the ACBD5-VAPB tether by FFAT motif phosphorylation and GSK3β.

Kors Suzan S Hacker Christian C Bolton Chloe C Maier Renate R Reimann Lena L Kitchener Emily J A EJA Warscheid Bettina B Costello Joseph L JL Schrader Michael M

The Journal of cell biology 20220112 3

Peroxisomes and the endoplasmic reticulum (ER) cooperate in cellular lipid metabolism. They form membrane contacts through interaction of the peroxisomal membrane protein ACBD5 (acyl-coenzyme A-binding domain protein 5) and the ER-resident protein VAPB (vesicle-associated membrane protein-associated protein B). ACBD5 binds to the major sperm protein domain of VAPB via its FFAT-like (two phenylalanines [FF] in an acidic tract) motif. However, molecular mechanisms, which regulate formation of thes ...[more]

PMID: 35019937

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