Dataset Information

Heterologous production of phosphorylated casein

ABSTRACT: The demand for milk proteins is on the rise, but sustainability concerns dictate a reduction of animal-based agriculture. Microbial cell factories can be a viable alternative, but their inability to phosphorylate recombinant caseins is a major bottleneck, since phosphorylation is needed for calcium binding and functionality. We propose a solution based on engineered bacterial protein kinases, which results in microbially produced caseins with the correct phosphorylation pattern and functional properties.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli

SUBMITTER: Carsten Jers

LAB HEAD: Ivan Mijakovic

PROVIDER: PXD057429 | Pride | 2025-07-04

REPOSITORIES: pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	transfer_99008_files_57851d93.zip	Other
	transfer_99011_files_3f83bb6e.zip	Other

Items per page:

1 - 2 of 2

Similar Datasets

Project description:During lactation, mammary epithelial secretory cells secrete huge amounts of milk from their apical side. The major milk proteins, the caseins, are secreted by exocytosis, while milk fat globules are released by budding, enwrapped by the plasma membrane. Due to the number and large size of milk fat globules, the membrane surface needed for their secretion might exceed that of the apical plasma membrane. In order to identify the cellular compartments that may provide membrane during the budding of milk fat globules, a large-scale proteomics analysis of both cytoplasmic lipid droplets and secreted milk fat globules membranes was performed in mouse cells. The differential analysis of the protein profiles of these two organelles strongly suggest that, in addition to the apical plasma membrane, at least the endoplasmic reticulum, the secretory vesicles containing caseins, and potentially the mitochondria contribute to the formation of the milk fat globule membrane. Moreover, the specific analysis of the membrane-associated as well as the raft-associated proteins reinforces this possibility and points to a role for lipid rafts in milk product secretion. The subcellular localization of several major proteins of the cytoplasmic lipid droplets or of the milk fat globule membrane was investigated by immunofluorescence in lactating mammary epithelial cells. Furthermore, the localization of GM1 ganglioside, a known marker of lipid rafts and of free cholesterol, showed a clear association with both cytoplasmic lipid droplets and secreted milk fat globules. Additionally, the presence of some SNARE proteins that may be involved in casein exocytosis and of two Rab GTPases on both cytoplasmic lipid droplets and milk fat globules was demonstrated by immunofluorescence. Altogether, our results provide evidence for a pivotal role of the endoplasmic reticulum as membrane contributor to milk fat globule budding, and suggest that some SNARE proteins may spatio-temporally coordinate the secretion of milk products.

Dataset Information

Heterologous production of phosphorylated casein

Dataset's files

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets