In:
PLOS ONE, Public Library of Science (PLoS), Vol. 17, No. 1 ( 2022-1-20), p. e0262138-
Abstract:
We previously revealed the origin of mammalian simple-type glycogen synthase kinase interaction protein (GSKIP), which served as a scavenger and a competitor in the Wnt signaling pathway during evolution. In this study, we investigated the conserved and nonconserved regions of the composite-type GSKIP by utilizing bioinformatics tools, site-directed mutagenesis, and yeast two-hybrid methods. The regions were denoted as the pre-GSK3β binding site, which is located at the front of GSK3β-binding sites. Our data demonstrated that clustered mitochondria protein 1 (CLU1), a type of composite-type GSKIP that exists in the mitochondria of all eukaryotic organisms, possesses the protein known as domain of unknown function 727 (DUF727), with a pre-GSK3β-binding site and a mutant GSK3β-binding flanking region. Another type of composite-type GSKIP, armadillo repeat containing 4 (ARMC4), which is known for cilium movement in vertebrates, contains an unintegrated DUF727 flanking region with a pre-GSK3β-binding site (115SPxF118) only. In addition, the sequence of the GSK3β-binding site in CLU1 revealed that Q126L and V130L were not conserved, differing from the ideal GSK3β-binding sequence of simple-type GSKIP. We further illustrated two exceptions, namely 70 kilodalton heat shock proteins (Hsp70/DnaK) and Mitofilin in nematodes, that presented an unexpected ideal GSK3β-binding region with a pre-GSK3β sequence; this composite-type GSKIP could only occur in vertebrate species. Furthermore, we revealed the importance of the pre-GSK3β-binding site (118F or 118Y) and various mutant GSK3β-binding sites of composite-type GSKIP. Collectively, our data suggest that the new composite-type GSKIP starts with a DUF727 domain followed by a pre-GSK3β-binding site, with the subsequent addition of the GSK3β-binding site, which plays vital roles for CLU1, Mitofilin, and ARMC4 in mitochondria and Wnt signaling pathways during evolution.
Type of Medium:
Online Resource
ISSN:
1932-6203
DOI:
10.1371/journal.pone.0262138
DOI:
10.1371/journal.pone.0262138.g001
DOI:
10.1371/journal.pone.0262138.g002
DOI:
10.1371/journal.pone.0262138.g003
DOI:
10.1371/journal.pone.0262138.g004
DOI:
10.1371/journal.pone.0262138.g005
DOI:
10.1371/journal.pone.0262138.g006
DOI:
10.1371/journal.pone.0262138.t001
DOI:
10.1371/journal.pone.0262138.s001
DOI:
10.1371/journal.pone.0262138.s002
DOI:
10.1371/journal.pone.0262138.s003
DOI:
10.1371/journal.pone.0262138.s004
DOI:
10.1371/journal.pone.0262138.s005
DOI:
10.1371/journal.pone.0262138.r001
DOI:
10.1371/journal.pone.0262138.r002
DOI:
10.1371/journal.pone.0262138.r003
DOI:
10.1371/journal.pone.0262138.r004
DOI:
10.1371/journal.pone.0262138.r005
DOI:
10.1371/journal.pone.0262138.r006
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2022
detail.hit.zdb_id:
2267670-3
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