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J Cell Sci. 2013 Dec 1;126(Pt 23):5500-12. doi: 10.1242/jcs.139295. Epub 2013 Oct 8.

STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER.

Author information

1
Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Functional Genomics and Cancer Department, 1 rue Laurent Fries, Illkirch, 67404, France.

Abstract

Inter-organelle membrane contacts sites (MCSs) are specific subcellular regions favoring the exchange of metabolites and information. We investigated the potential role of the late-endosomal membrane-anchored proteins StAR related lipid transfer domain-3 (STARD3) and STARD3 N-terminal like (STARD3NL) in the formation of MCSs involving late-endosomes (LEs). We demonstrate that both STARD3 and STARD3NL create MCSs between LEs and the endoplasmic reticulum (ER). STARD3 and STARD3NL use a conserved two phenylalanines in an acidic tract (FFAT)-motif to interact with ER-anchored VAP proteins. Together, they form an LE-ER tethering complex allowing heterologous membrane apposition. This LE-ER tethering complex affects organelle dynamics by altering the formation of endosomal tubules. An in situ proximity ligation assay between STARD3, STARD3NL and VAP proteins identified endogenous LE-ER MCS. Thus, we report here the identification of proteins involved in inter-organellar interaction.

KEYWORDS:

Endoplasmic reticulum; Endosome; MENTAL domain; MENTHO; MLN64; Membrane contact site; START domain

PMID:
24105263
DOI:
10.1242/jcs.139295
[Indexed for MEDLINE]
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