Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
Autor: | Sergei I. Bannykh, Gavin Gabreski, Anna Bielli, Meir Aridor, Charles J. Haney, Simon C. Watkins |
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Rok vydání: | 2005 |
Předmět: |
GTP'
Vesicular Transport Proteins GTPase Biology Guanosine triphosphate Endoplasmic Reticulum Catalysis 03 medical and health sciences chemistry.chemical_compound Cytosol Cricetinae Report Animals COPII Cells Cultured Research Articles Monomeric GTP-Binding Proteins 030304 developmental biology 0303 health sciences Hydrolysis Endoplasmic reticulum Vesicle 030302 biochemistry & molecular biology Cell Biology COP-Coated Vesicles Protein Structure Tertiary Rats Protein Transport Membrane Gene Expression Regulation chemistry Biochemistry Liposomes Biophysics Guanosine Triphosphate Hydrophobic and Hydrophilic Interactions hormones hormone substitutes and hormone antagonists Protein Binding |
Zdroj: | The Journal of Cell Biology |
ISSN: | 1540-8140 0021-9525 |
DOI: | 10.1083/jcb.200509095 |
Popis: | The mechanisms by which the coat complex II (COPII) coat mediates membrane deformation and vesicle fission are unknown. Sar1 is a structural component of the membrane-binding inner layer of COPII (Bi, X., R.A. Corpina, and J. Goldberg. 2002. Nature. 419:271–277). Using model liposomes we found that Sar1 uses GTP-regulated exposure of its NH2-terminal tail, an amphipathic peptide domain, to bind, deform, constrict, and destabilize membranes. Although Sar1 activation leads to constriction of endoplasmic reticulum (ER) membranes, progression to effective vesicle fission requires a functional Sar1 NH2 terminus and guanosine triphosphate (GTP) hydrolysis. Inhibition of Sar1 GTP hydrolysis, which stabilizes Sar1 membrane binding, resulted in the formation of coated COPII vesicles that fail to detach from the ER. Thus Sar1-mediated GTP binding and hydrolysis regulates the NH2-terminal tail to perturb membrane packing, promote membrane deformation, and control vesicle fission. |
Databáze: | OpenAIRE |
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