Specific subdomain localization of ER resident proteins and membrane contact sites resolved by electron microscopy

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Lak , B , Li , S , Belevich , I , Sree , S , Butkovic , R , Ikonen , E & Jokitalo , E 2021 , ' Specific subdomain localization of ER resident proteins and membrane contact sites resolved by electron microscopy ' , European Journal of Cell Biology , vol. 100 , no. 7-8 , 151180 . https://doi.org/10.1016/j.ejcb.2021.151180

Title: Specific subdomain localization of ER resident proteins and membrane contact sites resolved by electron microscopy
Author: Lak, Behnam; Li, Shiqian; Belevich, Ilya; Sree, Sreesha; Butkovic, Rebeka; Ikonen, Elina; Jokitalo, Eija
Contributor organization: Molecular and Integrative Biosciences Research Programme
Institute of Biotechnology
Helsinki Institute of Life Science HiLIFE
STEMM - Stem Cells and Metabolism Research Program
Department of Anatomy
Lipid Trafficking Lab
Biosciences
Electron Microscopy
Mitochondrial Morphogenesis
Date: 2021
Language: eng
Number of pages: 9
Belongs to series: European Journal of Cell Biology
ISSN: 0171-9335
DOI: https://doi.org/10.1016/j.ejcb.2021.151180
URI: http://hdl.handle.net/10138/340602
Abstract: The endoplasmic reticulum (ER) is a large, single-copy, membrane-bound organelle that comprises an elaborate 3D network of diverse structural subdomains, including highly curved tubules, flat sheets, and parts that form contacts with nearly every other organelle. The dynamic and complex organization of the ER poses a major challenge on understanding how its functioning - maintenance of the structure, distribution of its functions and communication with other organelles - is orchestrated. In this study, we resolved a unique localization profile within the ER network for several resident ER proteins representing a broad range of functions associated with the ER using immuno-electron microscopy and calculation of a relative labeling index (RLI). Our results demonstrated the effect of changing cellular environment on protein localization and highlighted the importance of correct protein expression level when analyzing its localization at subdomain resolution. We present new software tools for anonymization of images for blind analysis and for quantitative assessment of membrane contact sites (MCSs) from thin section transmission electron microscopy micrographs. The analysis of ERmitochondria contacts suggested the presence of at least three different types of MCSs that responded differently to changes in cellular lipid loading status.
Subject: ER subdomains
ER-mitochondria contact sites
SOAT1
Relative labeling index
Quantitative morphological analysis
MITOCHONDRIA-ASSOCIATED MEMBRANES
TO-TUBULE TRANSFORMATION
ENDOPLASMIC-RETICULUM
MECHANISMS
CELLS
MORPHOLOGY
VESICLES
ROUGH
MAM
1182 Biochemistry, cell and molecular biology
Peer reviewed: Yes
Rights: cc_by_nc_nd
Usage restriction: openAccess
Self-archived version: publishedVersion


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