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  Secretory cargo sorting by Ca2+-dependent Cab45 oligomerization at the trans-Golgi network

Crevenna, A. H., Blank, B., Maiser, A., Emin, D., Prescher, J., Beck, G., et al. (2016). Secretory cargo sorting by Ca2+-dependent Cab45 oligomerization at the trans-Golgi network. Journal of Cell Biology, 213(3), 305-314. doi:10.1083/jcb.201601089.

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 Creators:
Crevenna, Alvaro H.1, Author
Blank, Birgit2, Author              
Maiser, Andreas1, Author
Emin, Derya1, Author
Prescher, Jens1, Author
Beck, Gisela2, Author              
Kienzle, Christine2, Author              
Bartnik, Kira1, Author
Habermann, Bianca3, Author              
Pakdel, Mehrshad2, Author              
Leonhardt, Heinrich1, Author
Lamb, Don C.1, Author
von Blume, Julia2, Author              
Affiliations:
1external, ou_persistent22              
2von Blume, Julia / Molecular Basis of Protein Trafficking, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565173              
3Habermann, Bianca / Computational Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1832284              

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Free keywords: POLARIZED EPITHELIAL-CELLS; FLUORESCENT-PROBES; ADF/COFILIN; APPARATUS; PROTEINS; COMPLEX; ACTIN; YEAST; SPCA1Cell Biology;
 Abstract: Sorting and export of transmembrane cargoes and lysosomal hydrolases at the trans-Golgi network (TGN) are well understood. However, elucidation of the mechanism by which secretory cargoes are segregated for their release into the extracellular space remains a challenge. We have previously demonstrated that, in a reaction that requires Ca2+., the soluble TGN-resident protein Cab45 is necessary for the sorting of secretory cargoes at the TGN. Here, we report that Cab45 reversibly assembles into oligomers in the presence of Ca2+. These Cab45 oligomers specifically bind secretory proteins, such as COMP and LyzC, in a Ca2+-dependent manner in vitro. In intact cells, mutation of the Ca(2+-)binding sites in Cab45 impairs oligomerization, as well as COMP and LyzC sorting. Superresolution microscopy revealed that Cab45 colocalizes with secretory proteins and the TGN Ca2+ pump (SPCA1) in specific TGN microdomains. These findings reveal that Ca2+-dependent changes in Cab45 mediate sorting of specific cargo molecules at the TGN.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000376144900006
DOI: 10.1083/jcb.201601089
 Degree: -

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Title: Journal of Cell Biology
Source Genre: Journal
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Publ. Info: New York, NY : Rockefeller Institute Press
Pages: - Volume / Issue: 213 (3) Sequence Number: - Start / End Page: 305 - 314 Identifier: ISSN: 0021-9525
CoNE: https://pure.mpg.de/cone/journals/resource/991042742946024_1