PXD001024

PXD001024 is an original dataset announced via ProteomeXchange.

Title	The plasma membrane, casein-containing vesicles and endoplasmic reticulum are the main membrane contributors to milk fat globule membrane formation
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.
HostingRepository	PRIDE
AnnounceDate	2018-10-19
AnnouncementXML	Submission_2018-10-19_00:17:48.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD001024
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	HENRY CELINE
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	dehydrated residue; phosphorylated residue; monohydroxylated residue; acetylated residue; deaminated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2014-06-02 00:44:04	ID requested
⏵ 1	2018-10-19 00:17:49	announced

Honvo-Hou, é, to E, Henry C, Chat S, Layani S, Truchet S, The endoplasmic reticulum and casein-containing vesicles contribute to milk fat globule membrane. Mol Biol Cell, 27(19):2946-64(2016) [pubmed]

curator keyword: Biological

submitter keyword: Mouse, MFGM, LC-MS/MS

INRA_PAPPSO_Céline Henry
contact affiliation	PAPPSO,MICALIS,INRA, France
contact email	celine.henry@jouy.inra.fr
lab head
HENRY CELINE
contact affiliation	INRA
contact email	celine.henry@jouy.inra.fr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2018/10/PXD001024

PRIDE project URI

• PRIDE
  1. PXD001024
     1. Label: PRIDE project
     2. Name: The plasma membrane, casein-containing vesicles and endoplasmic reticulum are the main membrane contributors to milk fat globule membrane formation