Myristoylation Restricts Orientation of the GRASP Domain on Membranes and Promotes Membrane Tethering

The mammalian Golgi reassembly stacking protein (GRASP) proteins are Golgi-localized homotypic membrane tethers that organize Golgi stacks into a long, contiguous ribbon-like structure. It is unknown how GRASPs undergo trans pairing given that cis interactions between the proteins in the plane of th...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 289; no. 14; pp. 9683 - 9691
Main Authors:	Heinrich, Frank, Nanda, Hirsh, Goh, Haw Zan, Bachert, Collin, Lösche, Mathias, Linstedt, Adam D.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 04-04-2014 American Society for Biochemistry and Molecular Biology
Subjects:	Animals Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Fluorescence Golgi Humans Lipid Bilayers - chemistry Lipid Bilayers - metabolism Lipoylation Membrane Bilayer Membrane Biology Membrane Fusion Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Membrane Trafficking Membranes, Artificial Myristic Acid - chemistry Myristic Acid - metabolism Neutron Scattering Protein Structure, Tertiary Membrane Trafficking Fluorescence Golgi Membrane Bilayer Membrane Fusion Neutron Scattering
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