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Histochem Cell Biol. 2017 Apr;147(4):439-451. doi: 10.1007/s00418-016-1527-3. Epub 2016 Dec 20.

Functional characterisation of the YIPF protein family in mammalian cells.

Author information

1
School of Biology and Environmental Science, University College Dublin, Dublin 4, Ireland.
2
UCD Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Dublin 4, Ireland.
3
Department of Clinical Biochemistry, Faculty of Pharmacy, University of Ljubljana, Aškerčeva 7, 1000, Ljubljana, Slovenia.
4
School of Biomolecular and Biomedical Science, University College Dublin, Dublin 4, Ireland.
5
Department of Molecular Biosciences, Faculty of Life Sciences, Kyoto Sangyo University, Motoyama, Kamigamo, Kita, Kyoto, 603-8555, Japan.
6
School of Medicine and Medical Science, University College Dublin, Dublin 4, Ireland.
7
School of Biology and Environmental Science, University College Dublin, Dublin 4, Ireland. jeremy.simpson@ucd.ie.
8
UCD Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Dublin 4, Ireland. jeremy.simpson@ucd.ie.

Abstract

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.

KEYWORDS:

Golgi apparatus; Membrane traffic; Subcellular localisation; Transmembrane proteins; YIPF

PMID:
27999994
DOI:
10.1007/s00418-016-1527-3
[Indexed for MEDLINE]

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