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10.1242/jcs.195263 http://scihub22266oqcxt.onion/10.1242/jcs.195263 C5358331!5358331 !28137759     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28137759 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Cell+Sci 2017 ; 130 (5 ): 903-915 Nephropedia Template TP {{tp|p=28137759 |t=2017. Mouse Stbd1 is N-myristoylated and affects ER-mitochondria association and mitochondrial morphology |pdf=|usr=}}{{28137759 }} gab.com Text Mouse Stbd1 is N-myristoylated and affects ER-mitochondria association and mitochondrial morphology JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=28137759 #FOAvip 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. Twit Text FOAVip Mouse Stbd1 is N-myristoylated and affects ER-mitochondria association and mitochondrial morphology ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=28137759 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28137759 #FOAvip English Wikipedia <ref>{{Cite pmid|28137759 }}</ref> Mouse Stbd1 is N-myristoylated and affects ER-mitochondria association and mitochondrial morphology #MMPMID28137759 Demetriadou A ; Morales-Sanfrutos J ; Nearchou M ; Baba O ; Kyriacou K ; Tate EW ; Drousiotou A ; Petrou PP J Cell Sci 2017[Mar]; 130 (5 ): 903-915 PMID28137759 show ga 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. |Animals [MESH] |Endoplasmic Reticulum/*metabolism/ultrastructure [MESH] |Gene Silencing [MESH] |Glycogen/metabolism [MESH] |HEK293 Cells [MESH] |HeLa Cells [MESH] |Humans [MESH] |Intracellular Membranes/metabolism [MESH] |Membrane Proteins/*metabolism [MESH] |Mice [MESH] |Mitochondria/*metabolism/ultrastructure [MESH] |Muscle Proteins/*metabolism [MESH] |Myristic Acid/*metabolism [MESH]Mouse Stbd1 is N-myristoylated and affects ER-mitochondria association(epmc).pdf DeepDyve Pubget Overpricing