Imaging LDL receptor oligomerization during endocytosis using a co-internalization assay
Name
Ting_Zou LDLR submission.pdf
Description
Main article
Size
1.25 MB
Format
Adobe PDF
Checksum (MD5)
3dca978797002bfd16c8cae903c01244
Author(s)
Zou, Peng
Ting, Alice Y.
Date Issued
December 2010
Journal
ACS Chemical Biology
Publisher
American Chemical Society
Citation
Zou, Peng, and Alice Y. Ting. “Imaging LDL Receptor Oligomerization During Endocytosis Using a Co-internalization Assay.” ACS Chemical Biology 6.4 (2011): 308–313.
Version
Author's final manuscript
Abstract
Methods to probe receptor oligomerization are useful to understand the molecular mechanisms of receptor signaling. Here we report a fluorescence imaging method to determine receptor oligomerization state in living cells during endocytic internalization. The wild-type receptor is co-expressed with an internalization-defective mutant, and the internalization kinetics of each are independently monitored. If the receptor internalizes as an oligomer, then the wild-type and mutant isoforms will mutually influence each others’ trafficking properties, causing co-internalization of the mutant or co-retention of the wild-type at the cell surface. Using this approach, we found that the low density lipoprotein (LDL) receptor internalizes as an oligomer into cells, both in the presence and absence of LDL ligand. The internalization kinetics of the wild-type receptor are not changed by LDL binding. We also found that the oligomerization domain of the LDL receptor is located in its cytoplasmic tail.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1021/cb100361k
