Functional analysis of HAE in vitro auto-phosphorylation sites.

Isaiah Taylor (846370); Ying Wang (11406); Kati Seitz (846371); John Baer (846372); Stefan Bennewitz (846373); Brian P. Mooney (418500); John C. Walker (728449)

doi:10.1371/journal.pone.0147203.g002

Functional analysis of HAE in vitro auto-phosphorylation sites.

By Isaiah Taylor (846370), Ying Wang (11406), Kati Seitz (846371), John Baer (846372), Stefan Bennewitz (846373), Brian P. Mooney (418500) and John C. Walker (728449)

Abstract

A) Identified HAE auto-phosphorylation sites annotated on the amino acid sequence of the HAE intracellular domain. Conserved features of protein kinases, as well as the HAE specific juxtamembrane region and C-terminal tail, are annotated for reference. B) Ratio of mutant:wildtype in situ auto-phosphorylation levels of recombinant MBP-HAE mutants. N = 4 biological replicates. Wildtype is normalized to 1. Error bars represent the standard deviation. Tests for statistical significance were carried out by a one sample t-test. C) Representative stains for phosphorylation and total protein by Pro-Q Diamond and coomassie blue, respectively.</p

Topics: Biological Sciences, HAE activation segment residues exhibits, substrate specificity, HAESA, protein kinase activity, activation segment residue, modulates HAE activity, rlk, HAE protein kinase domain, analysis, activation segment phosphorylation site

Year: 2016

DOI identifier: 10.1371/journal.pone.0147203.g002

OAI identifier: oai:figshare.com:article/1638751

Provided by: FigShare

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Functional analysis of HAE <i>in vitro</i> auto-phosphorylation sites.

Abstract

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