Dataset Information

Identification of phosphorylation sites on purified recombinant protein Dynamin-like protein 1

ABSTRACT: Drp1 is a GTPase involves in mitochondrial division. The phosphorylation of Drp1 is reported to influence Drp1 activity. Two well known Drp1 phosphorylation sites have been identified. In here, we in vitro phosphorylate S579 site by ERK2 kinase on WT-Drp1 or S600D-Drp1 mutant and try to identify the phosphorylation by Mass Spec.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Ao Liu

LAB HEAD: Henry N. Higgs

PROVIDER: PXD046824 | Pride | 2024-06-16

REPOSITORIES: Pride

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			Action	DRS
	HiggsH_080323_01.raw	Raw
	HiggsH_080323_01.raw__F019696_.mzid.gz	Mzid
	HiggsH_080323_01.raw__F019696_.mzid_HiggsH_080323_01.raw__F019696_.MGF	Mzid
	HiggsH_080323_02.raw	Raw
	HiggsH_080323_02.raw__F019697_.mzid.gz	Mzid

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Publications

Effects of phosphorylation on Drp1 activation by its receptors, actin, and cardiolipin.

Liu Ao A Hatch Anna L AL Higgs Henry N HN

Molecular biology of the cell 20231129 2

Drp1 is a dynamin family GTPase required for mitochondrial and peroxisomal division. Oligomerization increases Drp1 GTPase activity through interactions between neighboring GTPase domains. In cells, Drp1 is regulated by several factors including Drp1 receptors, actin filaments, cardiolipin, and phosphorylation at two sites: S579 and S600. Commonly, phosphorylation of S579 is considered activating, while S600 phosphorylation is considered inhibiting. However, direct effects of phosphorylation on ...[more]

PMID: 38019609

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