Differential interaction patterns in binding assays between recombinant syntaxin 1 and synaptobrevin isoforms

FEBS Letters

Pérez-Brangulı́, Francesc¹  Ruiz-Montasell, Bonaventura¹  Blasi, Juan¹ 

[1] Departament de Biologia Cel·lular i Anatomia Patològica, Universitat de Barcelona, Campus de Bellvitge, C/ Feixa Llarga s/n., 08907 L'Hospitalet de Llobregat, Spain

关键词: SNARE protein;    Syntaxin;    SNAP-25;    Synaptobrevin;    Regulated exocytosis;    BCA;    bicinchoninic acid;    BSA;    bovine serum albumin;    ECL;    enhanced chemiluminescence;    IPTG;    isopropyl β-D-thiogalactopyranoside;    GST;    glutathione S-transferase;    NSF;    N-ethylmaleimide sensitive factor;    PBS;    phosphate buffered saline;    RT-PCR;    reverse transcription-polymerase chain reaction;    SNAP;    soluble NSF attachment proteins;    SNAP-25;    synaptosomal associated protein of 25 kDa;    v- and t-SNARE;    vesicle- and target-SNAP receptor;   

DOI  :  10.1016/S0014-5793(99)01120-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Syntaxin 1 and synaptobrevin play an essential role in synaptic vesicle exocytosis. Two isoforms for each of these proteins, syntaxin 1A and 1B and synaptobrevin 1 and 2, have been found in nerve endings. Previous morphological studies have revealed a characteristic co-localization of syntaxin 1 and synaptobrevin isoforms in nervous and endocrine systems; however, the physiological significance of differential distribution is not known. In the present study an in vitro assay has been used to study a possible isoform specific interaction between syntaxin and synaptobrevin isoforms. The results show that although both syntaxin 1A and 1B may interact with synaptobrevin 1 and 2, this interaction is not uniform, showing different affinity patterns depending on the syntaxin 1/synaptobrevin isoform combination. The addition of SNAP-25 increased the binding capacity of syntaxin and synaptobrevin isoforms without affecting specific interactions.

【 授权许可】

Unknown