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Super-resolution microscopy reveals compartmentalization of peroxisomal membrane proteins

Abstract:
Membrane-associated events during peroxisomal protein import processes play an essential role in peroxisome functionality. Many details of these processes are not known due to missing spatial resolution of technologies capable of investigating peroxisomes directly in the cell. Here, we present the use of super-resolution optical stimulated emission depletion microscopy to investigate with sub-60-nm resolution the heterogeneous spatial organization of the peroxisomal proteins PEX5, PEX14, and PEX11 around actively importing peroxisomes, showing distinct differences between these peroxins. Moreover, imported protein sterol carrier protein 2 (SCP2) occupies only a subregion of larger peroxisomes, highlighting the heterogeneous distribution of proteins even within the peroxisome. Finally, our data reveal subpopulations of peroxisomes showing only weak colocalization between PEX14 and PEX5 or PEX11 but at the same time a clear compartmentalized organization. This compartmentalization, which was less evident in cases of strong colocalization, indicates dynamic protein reorganization linked to changes occurring in the peroxisomes. Through the use of multicolor stimulated emission depletion microscopy, we have been able to characterize peroxisomes and their constituents to a yet unseen level of detail while maintaining a highly statistical approach, paving the way for equally complex biological studies in the future.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1074/jbc.M116.734038

Authors

More by this author
Institution:
University of Oxford
Division:
MSD
Department:
RDM
Sub department:
RDM - Investigative Medicine Division
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
RDM
Sub department:
RDM - Investigative Medicine Division
Role:
Author


Publisher:
American Society for Biochemistry and Molecular Biology
Journal:
Journal of biological chemistry More from this journal
Volume:
291
Issue:
33
Pages:
16948-16962
Publication date:
2016-06-16
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Pmid:
27311714


Language:
English
Keywords:
Pubs id:
pubs:631065
UUID:
uuid:d397889d-7788-4088-8cf1-6fb1b93d6667
Local pid:
pubs:631065
Source identifiers:
631065
Deposit date:
2017-03-18
ARK identifier:

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