期刊
EXPERIMENTAL CELL RESEARCH
卷 315, 期 2, 页码 348-356出版社
ELSEVIER INC
DOI: 10.1016/j.yexcr.2008.10.038
关键词
Membrane dipeptidase; Detergent-resistant membranes; Protein transport; Endoplasmic reticulum
资金
- German Research Council, Bonn, Germany [SFB 621, DFG Na 331/1-4]
- Bayer Healthcare, Leverkusen, Germany
Membrane microdomains are implicated in the trafficking and sorting of several membrane proteins. In particular GPI-anchored proteins cluster into Triton X-100 resistant, cholesterol- and sphingolipid-rich membrane microdomains and are sorted to the apical membrane. A growing body of evidence has pointed to the existence of other types of microdomains that are insoluble in detergents, such as Lubrol WX and Tween-20. Here, we report on the role of detergent-resistant membranes formed at early stages in the biosynthesis of membrane dipeptidase (MDP), a GPI-anchored protein, on its trafficking and sorting. Pulse-chase experiments revealed a retarded maturation rate of the GPI-anchor deficient mutant (MDP Delta GPI) as compared to the wild type protein (wtMDP). However, Golgi to cell surface delivery rate did not show a significant difference between the two variants. On the other hand, early biosynthetic forms of wtMDP were partially insoluble in Tween-20, while MDPAGPI was completely soluble. The lack of association of MDPAGPI with detergent-resistant membranes prior to maturation in the Golgi and the reduction in its trafficking rate strongly suggest the existence of an early trafficking control mechanisms for membrane Proteins operating at a level between the endoplasmic reticulum and the cis-Golgi. (C) 2008 Elsevier Inc. All rights reserved.
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