Whitley P, Grahn E, Kutay U, Rapoport T A, von Heijne G
Department of Biochemistry, Stockholm University, Sweden.
J Biol Chem. 1996 Mar 29;271(13):7583-6. doi: 10.1074/jbc.271.13.7583.
Synaptobrevin is a tail-anchored protein with a hydrophobic C-terminal transmembrane segment that inserts into the endoplasmic reticulum membrane independently of the SRP/Sec61p pathway. Here, we show that idealized hydrophobic segments composed of 11-17 leucines and 1 valine function as insertion signals in vitro, whereas shorter segments do not. These results suggest that there are no specific requirements beyond overall hydrophobicity for C-terminal endoplasmic reticulum insertion signals.
突触小泡蛋白是一种尾部锚定蛋白，其疏水的C末端跨膜片段可独立于信号识别颗粒/ Sec61p途径插入内质网膜。在此，我们表明由11 - 17个亮氨酸和1个缬氨酸组成的理想化疏水片段在体外可作为插入信号，而较短的片段则不能。这些结果表明，对于C末端内质网插入信号，除了整体疏水性外没有特定要求。
