Sorting nexin 10 induces giant vacuoles in mammalian cells.

The Journal of biological chemistry (2006-10-03)
Baoming Qin, Miao He, Xiao Chen, Duanqing Pei

Eukaryotic cells maintain a sophisticated network of intracellular membranous system to ensure the proper distribution and compartmentalization of cellular proteins critical for diverse functions such as cell division or cell-cell communication. Yet, little is known about the mechanism that regulates the homeostasis of this system. While analyzing the impact of sorting nexins on the trafficking of membrane type matrix metalloproteinases, we unexpectedly discovered that the expression of SNX10 induced the formation of giant vacuoles in mammalian cells. This vacuolizing activity is sensitive to mutations at the putative phosphoinositide 3-phosphate binding residue Arg(53). Domain-swap experiments with SNX3 demonstrate that the PX domain of SNX10 alone is insufficient to generate vacuoles and the downstream C-terminal domain is required for vacuolization. Brefeldin A, a chemical known to block the endoplasmic reticulum to Golgi transport, inhibited the vacuolization process. Together, these results suggest that SNX10 activity may be involved in the regulation of endosome homeostasis.

Product Number
Product Description

Anti-SNX10 antibody produced in rabbit, affinity isolated antibody
Anti-SNX10 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon


Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.