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Mass spectrometry analysis of the Skp1 and Cullin1 interactome in Leishmania infantum

ABSTRACT: Leishmania infantum is the causative agent of visceral leishmaniasis in Latin America, a lethal disease if misdiagnosed or left untreated. The ubiquitin proteasome system (UPS) is the main regulator of intracellular proteolysis in eukaryotes and is required for parasite's to life cycle and infection. E3 ubiquitin ligases play important role in UPS and Cullin-1-RING ligases (CRL1) are the largest and most researched family of E3 in eukaryotes. CRL1 complex is made up of SKP1, Cullin1, RBX1, and F-box proteins. This complex is poorly studied in Leishmania. We investigated the interactome of CRL1 complex in L. infantum combining in vitro and in cellulo experiments to identify the interactome of Cullin1 and SKP1 through affinity purification followed by mass spectrometry analysis.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Leishmania Infantum

TISSUE(S): Whole Body

SUBMITTER: Felipe Roberti Teixeira

LAB HEAD: Felipe Roberti Teixeira

PROVIDER: PXD051961 | Pride | 2024-07-01

REPOSITORIES: Pride

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			Action	DRS
	11nov_FelipeTeixeira_CUL1.msf	Msf
	11nov_FelipeTeixeira_CUL1.raw	Raw
	11nov_FelipeTeixeira_CUL2.msf	Msf
	11nov_FelipeTeixeira_CUL2.raw	Raw
	11nov_FelipeTeixeira_CUL3.msf	Msf

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