Functional characterisation of the YIPF protein family in mammalian cells

被引:21
作者
Kranjc, Tilen [1 ,2 ,6 ]
Dempsey, Eugene [1 ,2 ]
Cagney, Gerard [2 ,3 ]
Nakamura, Nobuhiro [4 ]
Shields, Denis C. [2 ,5 ]
Simpson, Jeremy C. [1 ,2 ]
机构
[1] Univ Coll Dublin, Sch Biol & Environm Sci, Dublin 4, Ireland
[2] Univ Coll Dublin, UCD Conway Inst Biomol & Biomed Res, Dublin 4, Ireland
[3] Univ Coll Dublin, Sch Biomol & Biomed Sci, Dublin 4, Ireland
[4] Kyoto Sangyo Univ, Fac Life Sci, Dept Mol Biosci, Kita Ku, Kyoto 6038555, Japan
[5] Univ Coll Dublin, Sch Med & Med Sci, Dublin 4, Ireland
[6] Univ Ljubljana, Dept Clin Biochem, Fac Pharm, Askerceva 7, Ljubljana 1000, Slovenia
基金
爱尔兰科学基金会;
关键词
YIPF; Transmembrane proteins; Subcellular localisation; Membrane traffic; Golgi apparatus; BREFELDIN-A; ENDOPLASMIC-RETICULUM; RETROGRADE TRANSPORT; GOLGI-APPARATUS; ER; BINDING; IDENTIFICATION; COMPLEX; INTERMEDIATE; LOCALIZATION;
D O I
10.1007/s00418-016-1527-3
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
In this study, we carry out a systematic characterisation of the YIPF family of proteins with respect to their subcellular localisation profile, membrane topology and functional effects on the endomembrane system. YIPF proteins primarily localise to the Golgi complex and can be grouped into trans-Golgi-localising YIPFs (YIPF1 and YIPF2) and cis-Golgi-localising YIPFs (YIPF3, YIPF4 and YIPF5), with YIPF6 and YIPF7 showing a broader profile being distributed throughout the Golgi stack. YIPF proteins have a long soluble N-terminal region, which is orientated towards the cytosol, followed by 5 closely stacked transmembrane domains, and a C terminus, orientated towards the lumen of the Golgi. The significance of YIPF proteins for the maintenance of the morphology of the Golgi was tested by RNA interference, revealing a number of specific morphological changes to this organelle on their depletion. We propose a role for this family of proteins in regulating membrane dynamics in the endomembrane system.
引用
收藏
页码:439 / 451
页数:13
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