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Commit 25f1775c authored by Davide Lagoa's avatar Davide Lagoa
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<div class="next-level"><a href="/search/result.php?tc=1.A.101.8">View Proteins belonging to: <span style="color:maroon;">The Peroxisomal Pore-forming Pex11 (Pex11) Family</span></a></div>
<!-- <div class="title">1.A.101: The Peroxisomal Pore-forming Pex11 (Pex11) Family</div> -->
<div class="description"><p style='text-align: center;'><strong>1.A.101 The Peroxisomal Pore-forming Pex11 (Pex11) Family</strong></p>
<p>More than thirty Pex proteins are known to participate in the biogenesis of peroxisomes, oxidative organelles involved in lipid and ROS metabolism. Pex11 homologues are constituents of the Pexoxisomal Protein Importer (PPI) Family (TC# 3.A.20). They play roles, direct or indirect, in division and proliferation of peroxisomes (<a class="reflink" href="/search/result.php?tc=1.A.101#ref34544772">Schrader <em>et al.</em> 1998</a>).&nbsp;<a class="reflink" href="/search/result.php?tc=1.A.101#ref34544773">Mindthoff <em>et al.</em> 2015</a> showed that yeast Pex11 is a
pore-forming protein, possibly sharing significant sequence similarity with TRPM cation-selective channels. The Pex11
channel is moderately cation-selective
(PK<sup>+</sup>/PCl<sup>-</sup>=1.85) and resistant to voltage-dependent closing. The estimated size of the channel's pore
(r~0.6nm) supports the notion that Pex11 conducts solutes with molecular mass below 300-400 Da, and the channel's selectivity filter was localized. Overproduction of Pex11 resulted in acceleration of
fatty acids beta-oxidation in intact cells but not in the corresponding lysates. Beta-oxidation in cells was affected by expression of the Pex11 protein carrying point mutations in the selectivity
filter. These data suggested that the Pex11-dependent transmembrane traffic of metabolites may be a
rate-limiting step in the beta-oxidation of fatty acids. This conclusion was corroborated by
analysis of the rate of beta-oxidation in yeast strains expressing Pex11 with mutations mimicking
constitutively phosphorylated (S165D, S167D) or unphosphorylated (S165A, S167A) protein. The results
suggest that phosphorylation of Pex11 is a mechanism that can control the peroxisomal beta-oxidation
rate.&nbsp; Pex11 is thus a non-selective channel responsible
for transfer of metabolites across peroxisomal membrane.(<a class="reflink" href="/search/result.php?tc=1.A.101#ref34544773">Mindthoff <em>et al.</em> 2015</a>).</p></div>
<div class="result-superfam">This family belongs to the:<a href="/superfamily.php?id=76"> Peroxisomal Peroxin (Pex)11/25/27 (Pex11/25/27) Superfamily</a>.</div>
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<h4>References associated with 1.A.101 family:</h4>
<div class="ref">
<div class=''>
<A ID="ref34545748"></A>Jaiteh, M., A. Taly, and J. Hénin. (2016). Evolution of Pentameric Ligand-Gated Ion Channels: Pro-Loop Receptors. PLoS One 11: e0151934. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=26986966" target="_window">26986966</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34544773"></A>Mindthoff S., Grunau S., Steinfort LL., Girzalsky W., Hiltunen JK., Erdmann R. and Antonenkov VD. (2015). Peroxisomal Pex11 is a pore-forming protein homologous to TRPM channels. Biochim Biophys Acta. 1863(2):271-283. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=26597702" target="_window">26597702</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34544772"></A>Schrader, M., B.E. Reuber, J.C. Morrell, G. Jimenez-Sanchez, C. Obie, T.A. Stroh, D. Valle, T.A. Schroer, and S.J. Gould. (1998). Expression of PEX11beta mediates peroxisome proliferation in the absence of extracellular stimuli. J. Biol. Chem. 273: 29607-29614. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=9792670" target="_window">9792670</A></div>
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<div class="next-level"><a href="/search/result.php?tc=1.A.102.1">View Proteins belonging to: <span style="color:maroon;">The Influenza A viroporin PB1-F2 (PB1-F2) Family</span></a></div>
<!-- <div class="title">1.A.102: The Influenza A viroporin PB1-F2 (PB1-F2) Family</div> -->
<div class="description"><p style='text-align: center;'><strong>1.A.102 The Influenza A viroporin PB1-F2 (PB1-F2) Family</strong></p>
<p>The PB1-F2 protein of 90 aas, and possibly a weakly hydrophobic C-terminal TMS, exhibits viroporin activity, transporting monovalent cations and Ca<sup>2+ </sup>(<a class="reflink" href="/search/result.php?tc=1.A.102#ref34545079">Hyser and Estes 2015</a>).&nbsp;</p></div>
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<h4>References associated with 1.A.102 family:</h4>
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<div class=''>
<A ID="ref34545080"></A>Hyser, J.M. and M.K. Estes. (2015). Pathophysiological Consequences of Calcium-Conducting Viroporins. Annu Rev Virol 2: 473-496. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=26958925" target="_window">26958925</A></div>
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<div class="next-level"><a href="/search/result.php?tc=1.A.103.1">View Proteins belonging to: <span style="color:maroon;">The Simian Virus 5 (Parainfluenza Virus 5) SH (SV5-SH) Family</span></a></div>
<!-- <div class="title">1.A.103: The Simian Virus 5 (Parainfluenza Virus 5) SH (SV5-SH) Family</div> -->
<div class="description"><p style='text-align: center;'><strong>1.A.103 The Simian Virus 5 (Parainfluenza Virus 5) SH (SV5-SH) Family</strong>&nbsp;</p>
<p>The SV5-SH family consists of short (44 aa) proteins with one C-terminal TMS that form viroporins that transport monovalent cations (<a class="reflink" href="/search/result.php?tc=1.A.103#ref34545079">Hyser and Estes 2015</a>).</p></div>
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<h4>References associated with 1.A.103 family:</h4>
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<div class=''>
<A ID="ref34545085"></A>Hyser, J.M. and M.K. Estes. (2015). Pathophysiological Consequences of Calcium-Conducting Viroporins. Annu Rev Virol 2: 473-496. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=26958925" target="_window">26958925</A></div>
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<div class="next-level"><a href="/search/result.php?tc=1.A.104.1">View Proteins belonging to: <span style="color:maroon;">The Proposed Flagellar Biosynthesis Na+ Channel, FlaH (FlaH) Family</span></a></div>
<!-- <div class="title">1.A.104: The Proposed Flagellar Biosynthesis Na+ Channel, FlaH (FlaH) Family</div> -->
<div class="description"><p style='text-align: center;'><strong>1.A.104 The Proposed Flagellar Biosynthesis Na<sup>+</sup> Channel, FlhA (FlhA) Family&nbsp;</strong></p>
<p>The flagellar type III export apparatus utilizes ATP and the proton motive force (PMF) to
transport flagellar proteins to the distal end of the growing flagellar structure for self-assembly.
The transmembrane export gate complex is a H<sup>+</sup>-protein antiporter. Activity is greatly
augmented by an associated cytoplasmic ATPase complex.&nbsp;<a class='reflink' href='../../search/#ref34545097'>Minamino <em>et al.</em> 2016</a> reported that the export gate complex
can use the sodium motive force (SMF) in addition to the PMF to drive
protein export. Protein export was considerably reduced in the absence of the ATPase complex and a
pH gradient across the membrane, but Na<sup>+</sup> increased it dramatically. Phenamil, a blocker of Na<sup>+</sup> translocation, inhibited protein export. Overexpression of FlhA increased the intracellular Na<sup>+</sup> concentration in the presence of 100 mM external NaCl but not in its absence, suggesting that FlhA acts as a
Na<sup>+</sup> channel. In wild-type cells, however, neither Na<sup>+</sup> nor phenamil affected protein export,
indicating that the Na<sup>+</sup> channel activity of FlhA is suppressed by the ATPase complex. <a class='reflink' href='../../search/#ref34545097'>Minamino <em>et al.</em> 2016</a> proposed
that the export gate by itself is a dual fuel engine that uses both the PMF and the SMF for protein export,
and that the ATPase complex switches this dual fuel engine into a PMF-driven export machinery to
become much more robust against environmental changes in external pH and Na<sup>+</sup> concentration.</p></div>
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<div class="next-level"><a href="/search/result.php?tc=1.A.104.1">View Proteins belonging to: <span style="color:maroon;">The Proposed Flagellar Biosynthesis Na+ Channel, FlaH (FlaH) Family</span></a></div>
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<h4>References associated with 1.A.104 family:</h4>
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<A ID="ref34545098"></A>Minamino, T., Y.V. Morimoto, N. Hara, P.D. Aldridge, and K. Namba. (2016). The Bacterial Flagellar Type III Export Gate Complex Is a Dual Fuel Engine That Can Use Both H<sup>+</sup> and Na<sup>+</sup> for Flagellar Protein Export. PLoS Pathog 12: e1005495. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=26943926" target="_window">26943926</A></div>
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