Association of Drosophila cysteine string proteins with membranes

FEBS Letters

van de Goor, Jana¹  Kelly, Regis B.¹ 

[1] Hormone Research Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-0534, USA

关键词: Cysteine string proteins;    Post-translational modification;    Drosophila;    Fatty acylation;    Synaptic vesicle;    Dcsp's;    Drosophila cysteine string proteins;    T-csp;    Torpedo cysteine string protein;   

DOI  :  10.1016/0014-5793(96)00026-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cysteine string proteins are putative synaptic vesicle proteins that lack a transmembrane domain. Our analysis shows that Drosophila cysteine string proteins are extensively modified by hydroxylamine-sensitive fatty acylation. This modification could be responsible for association of csp's with membranes. Extensive deacylation of Dcsp's by a 20 h incubation in 1 M hydroxylamine, pH 7.0, or methanolic KOH produces a protein of 6–7 kDa lower mass than untreated Dcsp's. Surprisingly, the hydroxylamine treatment does not cause release of Dcsp's from membranes. On the other hand, alkaline stripping of membranes isolated from Drosophila brain by 0.1 M sodium carbonate, pH 11.5, causes a significant release of Dcsp's from membranes into the cytosol. These results indicate that fatty acylation may not form the main anchor of Dcsp's in membranes. Taking advantage of the endocytotic block in the Drosophila mutant shibire ^ts1, we analyzed the acylation states of Dcsp's in two stages during synaptic vesicle recycling and found no evidence for an acylation/ deacylation cycle of Dcsp's in the brain nerve terminals.

【 授权许可】

Unknown