Extensive lipidation of a Torpedo cysteine string protein

Autor:	C B, Gundersen, A, Mastrogiacomo, K, Faull, J A, Umbach
Rok vydání:	1994
Předmět:	Electric Organ Xenopus Fatty Acids Palmitic Acid Membrane Proteins Nerve Tissue Proteins Palmitic Acids HSP40 Heat-Shock Proteins Torpedo Membrane Fusion Oocytes Animals Synaptic Vesicles Protein Processing Post-Translational
Zdroj:	The Journal of biological chemistry. 269(30)
ISSN:	0021-9258
Popis:	Cysteine string proteins are relatively low mass components of synaptic vesicle membranes. Structurally, their primary sequence is distinguished by a remarkable, cysteine-rich motif. Investigations revealed an unprecedented degree of lipidation of these cysteine residues. At least 11 of the 13 cysteines of the Torpedo protein were modified, principally by palmitoyl moieties. This fatty acylation creates a prominent hydrophobic domain flanked by polar amino and carboxyl termini. An amphipathic structure of this type is uniquely suited to mediate events at membrane interfaces. Thus, cysteine string proteins are candidates to participate in exocytotic membrane fusion.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::e50d56b31bcbf9ab652f3d9bdb891216 https://pubmed.ncbi.nlm.nih.gov/8034679 Zobrazit plný text záznamu