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Identification of MELK-mediated Cofilin-1 T70 phosphorylation by IP-LC-MS/MS analysis

ABSTRACT: To investigate whether MELK phosphorylates Cofilin-1 at residue Threonine 70 (T70), we performed a phosphoproteomic validation using immunoprecipitation coupled with mass spectrometry (IP-LC-MS/MS). HEK293T cells were divided into three experimental groups: (1) MOCK control (Empty Vector), (2) MELK overexpression, and (3) MELK overexpression treated with the inhibitor OTSSP167. Endogenous Cofilin-1 was enriched by immunoprecipitation. The study aimed to identify and quantify the phosphorylation status of Cofilin-1, specifically focusing on the T70 site, and to assess the impact of MELK kinase activity and its inhibition by OTSSP167 on this phosphorylation event.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Kuai Yu

LAB HEAD: Kuai Yu

PROVIDER: PXD074164 | Pride | 2026-04-01

REPOSITORIES: pride

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			Action	DRS
	EV_QK1_Slot1-15_1_28205.d.zip	Other
	MELK_OTSSP167_QK3_Slot1-17_1_28207.d.zip	Other
	MELK_QK2_Slot1-16_1_28206.d.zip	Other
	PhosphoSites.txt	Txt
	checksum.txt	Txt

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