A ZIP6-ZIP10 heteromer controls NCAM1 phosphorylation and integration into focal adhesion complexes during epithelial-to-mesenchymal transition View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-01-18

AUTHORS

Dylan Brethour, Mohadeseh Mehrabian, Declan Williams, Xinzhu Wang, Farinaz Ghodrati, Sepehr Ehsani, Elizabeth A. Rubie, James R. Woodgett, Jean Sevalle, Zhengrui Xi, Ekaterina Rogaeva, Gerold Schmitt-Ulms

ABSTRACT

The prion protein (PrP) evolved from the subbranch of ZIP metal ion transporters comprising ZIPs 5, 6 and 10, raising the prospect that the study of these ZIPs may reveal insights relevant for understanding the function of PrP. Building on data which suggested PrP and ZIP6 are critical during epithelial-to-mesenchymal transition (EMT), we investigated ZIP6 in an EMT paradigm using ZIP6 knockout cells, mass spectrometry and bioinformatic methods. Reminiscent of PrP, ZIP6 levels are five-fold upregulated during EMT and the protein forms a complex with NCAM1. ZIP6 also interacts with ZIP10 and the two ZIP transporters exhibit interdependency during their expression. ZIP6 contributes to the integration of NCAM1 in focal adhesion complexes but, unlike cells lacking PrP, ZIP6 deficiency does not abolish polysialylation of NCAM1. Instead, ZIP6 mediates phosphorylation of NCAM1 on a cluster of cytosolic acceptor sites. Substrate consensus motif features and in vitro phosphorylation data point toward GSK3 as the kinase responsible, and interface mapping experiments identified histidine-rich cytoplasmic loops within the ZIP6/ZIP10 heteromer as a novel scaffold for GSK3 binding. Our data suggests that PrP and ZIP6 inherited the ability to interact with NCAM1 from their common ZIP ancestors but have since diverged to control distinct posttranslational modifications of NCAM1. More... »

PAGES

40313

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep40313

DOI

http://dx.doi.org/10.1038/srep40313

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1015828884

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28098160


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63 focal adhesion complexes
64 function
65 heteromers
66 insights
67 integration
68 interdependencies
69 ion transporters
70 kinase
71 knockout cells
72 levels
73 loop
74 mapping experiments
75 mass spectrometry
76 mesenchymal transition
77 metal ion transporters
78 method
79 modification
80 motif
81 novel scaffold
82 paradigm
83 phosphorylation
84 point
85 polysialylation
86 posttranslational modifications
87 prion protein
88 prospects
89 protein
90 scaffolds
91 sites
92 spectrometry
93 study
94 subbranches
95 transition
96 transporters
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