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rab3效应结构域修饰肽对胞吐膜融合的刺激作用:对rab3在调节性胞吐作用中作用的重新评估

Stimulation of exocytotic membrane fusion by modified peptides of the rab3 effector domain: re-evaluation of the role of rab3 in regulated exocytosis.

作者信息

MacLean C M, Law G J, Edwardson J M

机构信息

Department of Pharmacology, University of Cambridge, U.K.

出版信息

Biochem J. 1993 Sep 1;294 ( Pt 2)(Pt 2):325-8. doi: 10.1042/bj2940325.

Abstract

We have shown previously that fusion between pancreatic zymogen granules and plasma membranes is stimulated by a peptide corresponding to the putative effector domain of rab3. Here we show that this stimulatory effect persists when the amino acid sequence of the peptide is substantially modified. We also show that an antibody raised against rab3a recognizes a protein of appropriate size on the zymogen-granule membrane, but has no effect on membrane fusion. We suggest that rab3 is not directly involved in the control of this membrane fusion event, and that the peptides are stimulating fusion by a mechanism unrelated to rab3.

摘要

我们之前已经表明,胰腺酶原颗粒与质膜之间的融合受到一种与rab3假定效应结构域相对应的肽的刺激。在此我们表明,当该肽的氨基酸序列被大幅修饰时,这种刺激作用仍然存在。我们还表明,针对rab3a产生的抗体可识别酶原颗粒膜上大小合适的一种蛋白质,但对膜融合没有影响。我们认为rab3并不直接参与这一膜融合事件的调控,并且这些肽是通过一种与rab3无关的机制刺激融合的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9664/1134456/8cb2ba5ad540/biochemj00104-0033-a.jpg

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