Dataset Information

Galectin-3 Mediated Endocytosis of the Orphan G-Protein-Coupled Receptor GPRC5A

ABSTRACT: Galectins, a family of glycan-binding proteins, play crucial roles in various cellular functions, acting both at intracellular and extracellular levels. Among them, Galectin-3 (Gal-3) stands out as a unique member, belonging to the chimera subfamily. Gal-3 recruitment of plasma membrane glycosylated cargo leads to clustering and membrane bending, ultimately resulting in the formation of endocytic invaginations. An interactomic analysis on endogenous Gal-3 identified the orphan G-protein coupled receptor GPRC5A as a new binding partner for Gal-3. GPRC5A is also termed RAI3 as its expression is induced by retinoic-acid. Our results also show that GPRC5A is internalized by addition of extracellular Gal-3 and that GPRC5A trafficking pathway goes via the early and the recycling endosomes. In SW480 colorectal cancer cells, the glycosylated forms of GPRC5A interact with Gal-3 and their levels were increased by all-trans retinoic-acid (ATRA) addition. In SW480 cells, endocytic internalization of endogenous GPRC5A was achieved by extracellular Gal-3 addition but not by ATRA. This study reveals insights into the endocytic mechanisms of GPRC5A for which no specific ligand is described. Further research in this direction may unveil additional Gal-3 mediated functions in GPRC5A cellular signaling and contribute to the development of innovative therapeutic approaches.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Johana Chicher

LAB HEAD: Sylvie Friant

PROVIDER: PXD048507 | Pride | 2025-10-09

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	2017_S39_Abdel_HEPG2-Ab-dil6.mgf	Mgf
	2017_S39_Abdel_HEPG2-Ab-dil6.raw	Raw
	2017_S39_Abdel_HEPG2withAb-dil6.mgf	Mgf
	2017_S39_Abdel_HEPG2withAb-dil6.raw	Raw
	2018_S08_Abdel_16032018-dil6_Ctl1.mgf	Mgf

Items per page:

1 - 5 of 32

Similar Datasets

Project description:Inducing the long-term protection via effector memory CD8+ T cells residing in the peripheral tissues is the ultimate goal of T cell-based vaccination strategies. CD8+ T cell reacting against a particular set of antigenic peptides show propensity to generate stable pools of memory inflating cells with profound protective capacity. While the epitopes that induce memory inflation have been thoroughly characterized and used as excellent constituents of vaccines such as recombinant adenoviruses, the identity of the tissue factors responsible for maintaining memory inflating CD8+ T cells remains elusive. Here, we have used a Cre recombinase-dependent, -galactosidase (gal)–recombinant adenovirus vector that allowed for cell-specific expression of gal epitopes and identification of cell types involved in generation of inflationary responses. While targeting antigen expression to classical hematopoietic antigen presenting cells was insufficient to activate gal-specific CD8+ T cells, expressing the antigen exclusively in CCL19-producing fibroblastic stromal cells (FSCs) induced robust anti-gal CD8+ T cell response. Using bone marrow chimera mice to abolish the expression of major histocompatibility complex I (MHC-I) and Basic Leucine Zipper ATF-Like Transcription Factor 3 (BATF3) in hematopoietic cells we demonstrated that CCL19-expressing FCS function as antigen libraries, gradually releasing the antigen to CD103+ DCs to maintain gal-specific memory inflating population. Moreover, targeted ablation of CCL19-producing cells revealed that pulmonary fibroblastic stromal cells act as the principal organizer of the nurturing niches that support the metabolic conversion in CD8+ T cells necessary for the generation of long-lasting protective inflationary responses. Overall, our data reveal a hitherto unknown function of CCL19-expressiong fibroblastic stromal in supporting the metabolic fitness of CD8+ T cells, thereby promoting the generation of tissue-specific and long-lasting protective CD8+ T cell responses.

Dataset Information

Galectin-3 Mediated Endocytosis of the Orphan G-Protein-Coupled Receptor GPRC5A

Dataset's files

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets