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@article{Demetriadou:2017:10.1242/jcs.195263,
author = {Demetriadou, A and Morales-Sanfrutos, J and Nearchou, M and Baba, O and Kyriacou, K and Tate, EW and Drousiotou, A and Petrou, PP},
doi = {10.1242/jcs.195263},
journal = {Journal of Cell Science},
pages = {903--915},
title = {Mouse Stbd1 is N-myristoylated and affects ER-mitochondria association and mitochondrial morphology},
url = {http://dx.doi.org/10.1242/jcs.195263},
volume = {130},
year = {2017}
}
TY - JOUR
AB - Starch binding domain-containing protein 1 (Stbd1) is a carbohydrate-binding protein that has been proposed to be a selective autophagy receptor for glycogen. Here, we show that mouse Stbd1 is a transmembrane endoplasmic reticulum (ER)-resident protein with the capacity to induce the formation of organized ER structures in HeLa cells. In addition to bulk ER, Stbd1 was found to localize to mitochondria-associated membranes (MAMs), which represent regions of close apposition between the ER and mitochondria. We demonstrate that N-myristoylation and binding of Stbd1 to glycogen act as major determinants of its subcellular targeting. Moreover, overexpression of non-myristoylated Stbd1 enhanced the association between ER and mitochondria, and further induced prominent mitochondrial fragmentation and clustering. Conversely, shRNA-mediated Stbd1 silencing resulted in an increase in the spacing between ER and mitochondria, and an altered morphology of the mitochondrial network, suggesting elevated fusion and interconnectivity of mitochondria. Our data unravel the molecular mechanism underlying Stbd1 subcellular targeting, support and expand its proposed function as a selective autophagy receptor for glycogen and uncover a new role for the protein in the physical association between ER and mitochondria.
AU - Demetriadou,A
AU - Morales-Sanfrutos,J
AU - Nearchou,M
AU - Baba,O
AU - Kyriacou,K
AU - Tate,EW
AU - Drousiotou,A
AU - Petrou,PP
DO - 10.1242/jcs.195263
EP - 915
PY - 2017///
SN - 1477-9137
SP - 903
TI - Mouse Stbd1 is N-myristoylated and affects ER-mitochondria association and mitochondrial morphology
T2 - Journal of Cell Science
UR - http://dx.doi.org/10.1242/jcs.195263
UR - http://hdl.handle.net/10044/1/44061
VL - 130
ER -
Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ
e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821