Dataset Information

Mass spectrometry-based analysis of kindlin phosphorylation, ubiquitination and interactome

ABSTRACT: Kindlin is an essential activator of integrins and thus indispensable in cell to extracellular matrix (ECM) adhesion. Kindlin abundance and functions are tightly regulated by multiple mechanisms including post-translational modifications (PTMs). Despite the critical roles of kindlin during embryonic development and pathogenesis, the knowledge of kindlin’s PTMs and interactome is far from complete. Here we analyze the phosphorylation, ubiquitination and interacting partners of kindlin in flat, firmly adherent interphase cells and round, weakly attached mitotic cells by immunoprecipitation-based mass spectrometry (IP-MS). The analysis generated potential phosphorylation and ubiquitination sites as well as interactors of kindlin and paved the way to investigate PTMs and binding partners of kindlin.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

SUBMITTER: Nanpeng Chen

LAB HEAD: Reinhard Fässler

PROVIDER: PXD031829 | Pride | 2022-02-22

REPOSITORIES: Pride

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			Action	DRS
	20190729_coreQEP1_NiKr_LC12-19_SA_Orbi3283Sample01.raw	Raw
	20190729_coreQEP1_NiKr_LC12-19_SA_Orbi3283Sample02.raw	Raw
	20190729_coreQEP1_NiKr_LC12-19_SA_Orbi3283Sample03.raw	Raw
	20190729_coreQEP1_NiKr_LC12-19_SA_Orbi3283Sample04.raw	Raw
	20190729_coreQEP1_NiKr_LC12-19_SA_Orbi3283Sample05.raw	Raw

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Mass spectrometry-based analysis of kindlin phosphorylation, ubiquitination and interactome

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