Mouse Stbd1 is N -myristoylated and affects ER-mitochondria association and mitochondrial morphology

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 or...

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Published inJournal of cell science Vol. 130; no. 5; pp. 903 - 915
Main Authors Demetriadou, Anthi, Morales-Sanfrutos, Julia, Nearchou, Marianna, Baba, Otto, Kyriacou, Kyriacos, Tate, Edward W, Drousiotou, Anthi, Petrou, Petros P
Format Journal Article
LanguageEnglish
Published England The Company of Biologists Ltd 01.03.2017
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Abstract 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 -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.
AbstractList 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 -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.
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. Highlighted Article: The glycogen-binding protein Stbd1 is N -myristoylated and targeted to ER–mitochondria contact sites. Stbd1 loss- or gain-of-function affects ER–mitochondria association and mitochondrial morphology.
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.
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.Highlighted Article: The glycogen-binding protein Stbd1 is N-myristoylated and targeted to ER–mitochondria contact sites. Stbd1 loss- or gain-of-function affects ER–mitochondria association and mitochondrial morphology.
Author Demetriadou, Anthi
Nearchou, Marianna
Drousiotou, Anthi
Baba, Otto
Morales-Sanfrutos, Julia
Tate, Edward W
Petrou, Petros P
Kyriacou, Kyriacos
AuthorAffiliation 1 Department of Biochemical Genetics , The Cyprus Institute of Neurology and Genetics , P. O. Box 23462, Nicosia 1683 , Cyprus
2 The Cyprus School of Molecular Medicine, P. O. Box 23462 , Nicosia 1683 , Cyprus
5 Oral and Maxillofacial Anatomy, Faculty of Dentistry , Tokushima University , Tokushima 770-8504 , Japan
3 Department of Chemistry , Imperial College London , Exhibition Road, London SW7 2AZ , UK
4 Department of Electron Microscopy / Molecular Pathology , The Cyprus Institute of Neurology and Genetics , P. O. Box 23462, Nicosia 1683 , Cyprus
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Issue 5
Keywords N-myristoylation
Organized smooth endoplasmic reticulum
Mitochondria
Glycogen
Mitochondria-associated membranes
Stbd1
Endoplasmic reticulum
Language English
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Snippet Starch binding domain-containing protein 1 (Stbd1) is a carbohydrate-binding protein that has been proposed to be a selective autophagy receptor for glycogen....
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StartPage 903
SubjectTerms Animals
Apposition
Autophagy
Binding
Carbohydrates
Clustering
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Endoplasmic Reticulum - ultrastructure
Gene Silencing
Glycogen
Glycogen - metabolism
HEK293 Cells
HeLa Cells
Humans
Intracellular Membranes - metabolism
Membrane Proteins - metabolism
Membranes
Mice
Mitochondria
Mitochondria - metabolism
Mitochondria - ultrastructure
Morphology
Muscle Proteins - metabolism
Myristic Acid - metabolism
Myristoylation
Phagocytosis
Proteins
Starch
Subcellular Fractions - metabolism
Title Mouse Stbd1 is N -myristoylated and affects ER-mitochondria association and mitochondrial morphology
URI https://www.ncbi.nlm.nih.gov/pubmed/28137759
https://www.proquest.com/docview/1983433518
https://search.proquest.com/docview/1863218604
https://pubmed.ncbi.nlm.nih.gov/PMC5358331
Volume 130
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