Tang B L, Low D Y, Tan A E, Hong W
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore, Republic of Singapore.
Biochem Biophys Res Commun. 1998 Jan 14;242(2):345-50. doi: 10.1006/bbrc.1997.7966.
We have cloned a new member of the syntaxin family of proteins, designated human syntaxin 10 (hsyn10). The open reading frame encodes a polypeptide of 249 amino acids with potential coiled-coil domains and a carboxy-terminal hydrophobic tail. hsyn10 is particularly homologous to the recently reported rat syntaxin 6 (about 60% identity). Northern blot analysis showed that the transcript is enriched in the heart, skeletal muscles and pancreas. Indirect immunofluorescence studies using polyclonal antibodies raised against recombinant protein showed that the protein is localized to intracellular membrane structures, with perinuclear staining patterns colocalising well with the Golgi SNARE GS28. Morphological alterations of the staining pattern of the protein with brefeldin A but not wortmannin treatment indicate that the protein is localize to the trans-Golgi network.
我们克隆了Syntaxin蛋白家族的一个新成员,命名为人类Syntaxin 10(hsyn10)。开放阅读框编码一个由249个氨基酸组成的多肽,该多肽具有潜在的卷曲螺旋结构域和羧基末端疏水尾。hsyn10与最近报道的大鼠Syntaxin 6特别同源(约60%的同一性)。Northern印迹分析表明,该转录本在心脏、骨骼肌和胰腺中富集。使用针对重组蛋白产生的多克隆抗体进行的间接免疫荧光研究表明,该蛋白定位于细胞内膜结构,核周染色模式与高尔基体SNARE蛋白GS28共定位良好。用布雷菲德菌素A而非渥曼青霉素处理后,该蛋白染色模式的形态学改变表明该蛋白定位于反式高尔基体网络。