Title : Characterization of
YIPF3 and
YIPF4 ,
cis-Golgi Localizing Yip domain family
proteins
Abstract :
- The Yip1 domain family ( YIPF ) proteins are homologues of yeast Yip1p and Yif1p , which are proposed to function in ER to Golgi transport
- Here, we report the characterization of YIPF3 and YIPF4 , homologues of human Yif1p and Yip1p , respectively
- Immunofluorescence and immuno-electron microscopy showed that both YIPF3 and YIPF4 are clearly concentrated in the cis-Golgi
- While YIPF4 was detected as a single mobility form consistent with its predicted molecular weight, three different mobility forms of YIPF3 were detected by western blotting
- Biochemical and immunofluorescence experiments strongly indicated that YIPF3 is synthesized in the ER as a N-glycosylated form (40 kDa), is then O-glycosylated in the Golgi apparatus to become a lower mobility form (46 kDa) and finally becomes a higher mobility form cleaved at its C-terminal luminal domain (36 kDa)
- YIPF3 and YIPF4 form a complex in the Golgi apparatus, and this was suggested to be important for their proper localization and function
- The knockdown of YIPF3 or YIPF4 in HeLa cells induced fragmentation of the Golgi apparatus, suggesting their involvement in the maintenance of the Golgi structure
Output (sent_index, trigger,
protein,
sugar,
site):
- 5. N-glycosylated, , YIPF3, -, -
- 5. O-glycosylated, , YIPF3, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):