Pregled bibliografske jedinice broj: 824700
Late endosomal trafficking and endosecretory recycling route of open MHC-I conformers
Late endosomal trafficking and endosecretory recycling route of open MHC-I conformers // Abstract book
Beč, Austrija, 2015. str. 246-247 (poster, nije recenziran, sažetak, znanstveni)
CROSBI ID: 824700 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Late endosomal trafficking and endosecretory recycling route of open MHC-I conformers
Autori
Mahmutefendić, Hana ; Blagojević Zagorac G, Gordana ; Grabušić, Kristina ; Karleuša, Ljerka ; Momburg, Frank ; Lučin, Pero
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Abstract book
/ - , 2015, 246-247
Skup
4th European Congress of Immunology - ECI 2015
Mjesto i datum
Beč, Austrija, 06.09.2015. - 09.09.2015
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
opem MHC-I conformers; late endosomes; endocytosis
Sažetak
Open Major Histocompatibility Class I (MHC-I) conformers are cell surface proteins that segregate from fully conformed MHC-I proteins at the cell surface and travel late endosomal (LE) route after constitutive endocytic uptake. In this work, we have characterized LE trafficking route of open Ld molecules (empty Ld) in murine fibroblast-like cells. By using confocal microscopy, we have demonstrated that empty Ld enter the major Rab7-/NPC1-positive LE network either via Rab9-positive early late endosomes (LEs), together with M6PR, or via MLN64-positive early LEs, together with degradative cargo. In the major LE network empty Ld segregate into specific pre-degradative subset of LEs and enter either into degradative route or into endosecretory route and recycle back to the cell surface. The half-life of internalized empty Ld molecules is about 45-60 minutes (detected by flow cytometry or western blot analysis after surface biotynilation). That implies that molecules could be retained in endosomes. A fraction of empty Ld is segregated into the subset of endosecretory organelles that is distinct from exosome-generating endosecretory carriers. Segregation of empty Ld into degradative endosomes and degradation requires Rab7 and vectoral LE motility, whereas segregation into endosecretory carriers and recycling requires vectorial LE movements and cholesterol unloading but not Rab7. Thus, our analysis of empty Ld LE trafficking reveals endosecretory route and LE recycling of a plasma membrane protein. Analysis of LE eLd trafficking contributes to the understanding of the complexity of LE subsets and LE sorting, conformation based sorting in the endosomal system and the pathways of endosomal antigen-presentation.
Izvorni jezik
Engleski
Znanstvena područja
Temeljne medicinske znanosti
POVEZANOST RADA
Ustanove:
Medicinski fakultet, Rijeka
Profili:
Gordana Blagojević Zagorac
(autor)
Hana Mahmutefendić Lučin
(autor)
Ljerka Karleuša
(autor)
Pero Lučin
(autor)