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Article

Phosphorylation of C-terminal polycystin-2 influences the interaction with PIGEA14: a QCM study based on solid supported membranes.

Biochemical and biophysical research communications - 9 Aug 2013

Morick Daniela, Schatz Michaela, Hubrich Raphael, Hoffmeister Helen, Krefft Anya, Witzgall Ralph, Steinem Claudia

Abstract excerpt

Polycystin-2 (PC2) trafficking has been proposed to be a result of the interaction of PIGEA14 with PC2 as a function of the phosphorylation state of PC2. Here, we investigated the interaction of PIGEA14 with the C-terminal part of polycystin-2 wild type (cPC2wt) and the pseudophosphorylated mutant (cPC2S812D) to first, quantify the binding affinity between cPC2 and PIGEA14 and second, to elucidate the influence...

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PMID: 23838289
DOI: 10.1016/j.bbrc.2013.06.105

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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