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Commit 6961b5be authored by Davide Lagoa's avatar Davide Lagoa
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<div class="next-level"><a href="/search/result.php?tc=1.A.107.1">View Proteins belonging to: <span style="color:maroon;">The Pore-forming Globin (Globin) Family</span></a></div>
<!-- <div class="title">1.A.107: The Pore-forming Globin (Globin) Family</div> -->
<div class="description"><p style='text-align: center;'><strong>1.A.107 The Pore-forming Globin (Globin) Family&nbsp;</strong></p>
<p>Globins contain one or more cavities that control or affect such functions as ligand movement and
ligand binding. <a class="reflink" href="/search/result.php?tc=1.A.107#ref34545822">Morrill and Kostellow 2016</a> reported that the extended globin family [cytoglobin (Cygb); neuroglobin
(Ngb); myoglobin (Mb); hemoglobin (Hb) subunits Hba(alpha); and Hbb(beta)] contain either a
transmembrane (TM) helix or pore-lining region as well as internal cavities. Protein motif/domain
analyses indicate that Ngb and Hbb each contain 5 cholesterol-binding (CRAC/CARC) domains and 1
caveolin binding motif, whereas the Cygb dimer has 6 cholesterol-binding domains but lacks caveolin-
binding motifs. Mb and Hba each exhibit 2 cholesterol-binding domains and also lack caveolin-binding
motifs. The Hb &alpha;&beta;-tetramer contains 14 cholesterol-binding domains. Computer algorithms
indicate that Cygb and Ngb cavities display multiple partitions and C-terminal pore-lining regions,
whereas Mb has three major cavities plus a C-terminal pore-lining region. The Hb tetramer exhibits a
large internal cavity but the subunits differ in that they contain a C-terminal TM helix (Hba) and
pore-lining region (Hbb). The cavities include 43 of 190 Cygb residues, 38 of 151 of Ngb residues,
55 of 154 Mb residues, and 137 of 688 residues in the Hb tetramer. Each cavity complex includes 6 to
8 residues of the TM helix or pore-lining region and CRAC/CARC domains exist within all cavities.
Erythrocyte Hb &alpha;&beta;-tetramers are largely cytosolic but also bind to a membrane anion exchange
protein, 'band 3,' which contains a large internal cavity and 12 TM helices (5 being pore-lining
regions). The Hba TM helix may be the erythrocyte membrane 'band 3' attachment site. 'Band 3'
contributes 4 caveolin binding motifs and 10 CRAC/CARC domains. Cholesterol binding may create
lipid-disordered phases that alter globin cavities and facilitate ligand movement, permitting ion
channel formation and conformational changes that orchestrate anion and ligand (O2, CO2, NO)
movement within the large internal cavities and channels of the globins (<a class="reflink" href="/search/result.php?tc=1.A.107#ref34545822">Morrill and Kostellow 2016</a>).</p></div>
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<h4>References associated with 1.A.107 family:</h4>
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<div class=''>
<A ID="ref34545822"></A>Morrill, G.A. and A.B. Kostellow. (2016). Molecular Properties of Globin Channels and Pores: Role of Cholesterol in Ligand Binding and Movement. Front Physiol 7: 360. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=27656147" target="_window">27656147</A></div>
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<!-- <div class="title">1.A.108: The Fibroblast Growth Factor 2 (FGF2) Family</div> -->
<div class="description"><p style='text-align: center;'><strong>1.A.108.&nbsp; The Fibroblast Growth Factor 2 (FGF2) Family</strong></p>
<p>Unconventional secretory proteins lack signal peptides and their export
from cells is not affected by brefeldin A, an inhibitor of protein
transport along the classical secretory pathway (<a class="reflink" href="/search/result.php?tc=1.A.108#ref34546949">Nickel 2010</a>). Export can be mediated by direct
translocation across plasma membranes of cytoplasmic proteins such as <span class='highlight'>fibroblast growth factor 2</span> which can be modified by phosphorylation involving the Tec protein kinase (<a class="reflink" href="/search/result.php?tc=1.A.108#ref34546955">La Venuta <em>et al.</em> 2016</a>) so that it inserts into membranes, creating oligomeric pores that are intermediates in the secretion process (see&nbsp;<a class="reflink" href="/search/result.php?tc=1.A.108#ref34546951">Nickel and Seedorf 2008</a> and TC# 9.A.48). Tyrosyl phosphorylation of FGF2 followed by association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) triggers formation of a lipidic membrane pore, essential for FGF2 secretion (<a class="reflink" href="/search/result.php?tc=1.A.108#ref34546950">Steringer <em>et al.</em> 2012</a>). Formation of disulfide bridges is also essential for this process (<a class="reflink" href="/search/result.php?tc=1.A.108#ref34546952">M&uuml;ller <em>et al.</em> 2015</a>). The cytoplasmic domain of the Na+/K+ ATPase, ATP1A1 (&alpha;-subunit) may function as a direct interaction receptor for the process (<a class="reflink" href="/search/result.php?tc=1.A.108#ref34546953">Zacherl <em>et al.</em> 2015</a>). Extracellular FGF2 is trapped by cell surface proteoglycans, and it then plays a role in tumor-indiced angiogenesis (<a class="reflink" href="/search/result.php?tc=1.A.108#ref34546954">La Venuta <em>et al.</em> 2015</a>). Proteoglycans may also play a role in the secretion of the cytoskeletal Alzheimer's disease-associated tau protein (P10636; <a class="reflink" href="/search/result.php?tc=1.A.108#ref34546960">Pompa <em>et al.</em> 2017</a>). Tau secretion correlated with tau phosphorylation and aggregation (<a class="reflink" href="/search/result.php?tc=1.A.108#ref34546962">Hannan <em>et al.</em> 2016</a>).</p>
<p>Alpha-Klotho (&alpha;-Klotho) is a member of the Klotho family consisting of this protein and two other single-pass transmembrane proteins: betaKlotho (&beta;-Klotho) and gammaKlotho (&gamma;-Klotho); &alpha;-Klotho circulates in the blood. FGF23 is a member of the FGF superfamily of 22 genes/proteins. &alpha;-Klotho serves as a co-receptor with FGF receptors (FGFRs) to provide a receptacle for physiological FGF23 signaling, including regulation of phosphate metabolism (<a class="reflink" href="/search/result.php?tc=1.A.108#ref34549093">Hu <em>et al.</em> 2018</a>). The extracellular domain of transmembrane &alpha;-Klotho is shed by secretases and released into blood circulation (soluble &alpha;-Klotho). Soluble alphaKlotho has both FGF23-independent and FGF23-dependent roles in phosphate homeostasis by modulating intestinal phosphate absorption, urinary phosphate excretion, and phosphate distribution into bone in concerted interactions with other calciophosphotropic hormones such as PTH and 1,25-(OH)2D. The direct role of alphaKlotho and FGF23 in the maintenance of phosphate homeostasis is partly mediated by modulation of type II Na<sup>+</sup>-dependent phosphate co-transporters in target organs. alphaKlotho and FGF23 are principal phosphotropic hormones, and manipulation of the alphaKlotho-FGF23 axis provides a therapeutic strategy for genetic and acquired phosphate disorders and for conditions with FGF23 excess or alphaKlotho deficiency such as chronic kidney disease (<a class="reflink" href="/search/result.php?tc=1.A.108#ref34549184">Hu <em>et al.</em> 2018</a>).</p></div>
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<div class="tcdb-fam-ref">
<h4>References associated with 1.A.108 family:</h4>
<div class="ref">
<div class=''>
<A ID="ref34546962"></A>Hannan, S.B., N.M. Dräger, T.M. Rasse, A. Voigt, and T.R. Jahn. (2016). Cellular and molecular modifier pathways in tauopathies: the big picture from screening invertebrate models. J Neurochem 137: 12-25. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=26756400" target="_window">26756400</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34549184"></A>Hu, M.C., M. Shi, and O.W. Moe. (2018). Role of αKlotho and FGF23 in regulation of type II Na-dependent phosphate co-transporters. Pflugers Arch. [Epub: Ahead of Print] <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=30506274" target="_window">30506274</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34546954"></A>La Venuta, G., M. Zeitler, J.P. Steringer, H.M. Müller, and W. Nickel. (2015). The Startling Properties of Fibroblast Growth Factor 2: How to Exit Mammalian Cells without a Signal Peptide at Hand. J. Biol. Chem. 290: 27015-27020. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=26416892" target="_window">26416892</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34546955"></A>La Venuta, G., S. Wegehingel, P. Sehr, H.M. Müller, E. Dimou, J.P. Steringer, M. Grotwinkel, N. Hentze, M.P. Mayer, D.W. Will, U. Uhrig, J.D. Lewis, and W. Nickel. (2016). Small Molecule Inhibitors Targeting Tec Kinase Block Unconventional Secretion of Fibroblast Growth Factor 2. J. Biol. Chem. 291: 17787-17803. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=27382052" target="_window">27382052</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34546952"></A>Müller, H.M., J.P. Steringer, S. Wegehingel, S. Bleicken, M. Münster, E. Dimou, S. Unger, G. Weidmann, H. Andreas, A.J. García-Sáez, K. Wild, I. Sinning, and W. Nickel. (2015). Formation of disulfide bridges drives oligomerization, membrane pore formation, and translocation of fibroblast growth factor 2 to cell surfaces. J. Biol. Chem. 290: 8925-8937. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=25694424" target="_window">25694424</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34546949"></A>Nickel, W. (2010). Pathways of unconventional protein secretion. Curr Opin Biotechnol 21: 621-626. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=20637599" target="_window">20637599</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34546951"></A>Nickel, W. and M. Seedorf. (2008). Unconventional mechanisms of protein transport to the cell surface of eukaryotic cells. Annu. Rev. Cell Dev. Biol. 24: 287-308. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=18590485" target="_window">18590485</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34546961"></A>Pompa, A., F. De Marchis, M.T. Pallotta, Y. Benitez-Alfonso, A. Jones, K. Schipper, K. Moreau, V. Žárský, G.P. Di Sansebastiano, and M. Bellucci. (2017). Unconventional Transport Routes of Soluble and Membrane Proteins and Their Role in Developmental Biology. Int J Mol Sci 18:. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=28346345" target="_window">28346345</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34547513"></A>Smith, E.R., S.G. Holt, and T.D. Hewitson. (2017). FGF23 activates injury-primed renal fibroblasts via FGFR4-dependent signalling and enhancement of TGF-β autoinduction. Int J Biochem. Cell Biol. 92: 63-78. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=28919046" target="_window">28919046</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34546950"></A>Steringer, J.P., S. Bleicken, H. Andreas, S. Zacherl, M. Laussmann, K. Temmerman, F.X. Contreras, T.A. Bharat, J. Lechner, H.M. Müller, J.A. Briggs, A.J. García-Sáez, and W. Nickel. (2012). Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2)-dependent oligomerization of fibroblast growth factor 2 (FGF2) triggers the formation of a lipidic membrane pore implicated in unconventional secretion. J. Biol. Chem. 287: 27659-27669. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=22730382" target="_window">22730382</A></div>
</div>
<div class="ref">
<div class=''>
<A ID="ref34546953"></A>Zacherl, S., G. La Venuta, H.M. Müller, S. Wegehingel, E. Dimou, P. Sehr, J.D. Lewis, H. Erfle, R. Pepperkok, and W. Nickel. (2015). A direct role for ATP1A1 in unconventional secretion of fibroblast growth factor 2. J. Biol. Chem. 290: 3654-3665. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=25533462" target="_window">25533462</A></div>
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<div class="print-format"><img src="../images/printer.png" width="16"><A HREF="/tcfamilybrowse.php?tc=1.A.109" target="_window" border="0">Format for Printing</A></div>
<div class="next-level"><a href="/search/result.php?tc=1.A.109.1">View Proteins belonging to: <span style="color:maroon;">The Interleukin 1 (IL1) Family</span></a></div>
<!-- <div class="title">1.A.109: The Interleukin 1 (IL1) Family</div> -->
<div class="description"><p style='text-align: center;'><strong>1.A.109.&nbsp; The Interleukin 1 (IL1) Family&nbsp; </strong></p>
<p>Interleukin 1&alpha;, IL1A or IL1&alpha;, is p<span>roduced by activated macrophages, and IL-1 isoforms
stimulate thymocyte proliferation by inducing IL-2 release.
IL-1 proteins are involved in the inflammatory response, being
identified as endogenous pyrogens, and are reported to stimulate the
release of prostaglandin and collagenase from synovial cells.&nbsp; They also </span>disrupt the sertoli cell barrier/blood-testis
barrier by blocking Cx43 (TC# 1.A.24.1.1)-dependent gap junction communication (<a class="reflink" href="/search/result.php?tc=1.A.109#ref34546299">Chojnacka <em>et al.</em> 2016</a>)</p>
<p>Extracellular Interleukin-1&beta; (IL-1&beta;, IL1B, IL1F2), which regulates of the inflammatory
response, is secreted depending on the processing of a
precursor form following the activation of the multimolecular
inflammasome complex (see TC# 9.A.48). The secretion of IL-1&beta; after inflammasome activation requires
membrane permeabilization and occurs in parallel with the death of the
secreting cell. In macrophages, the release of IL-1&beta; in response to
inflammasome activation appears to be a secretory process independent
of nonspecific leakage of proteins during cell death. The mechanism of
membrane permeabilization leading to IL-1&beta; release is distinct from the
unconventional secretory mechanism employed by its structural homologues
fibroblast growth factor 2 (FGF2) or IL-1&alpha;, a process that involves the
formation of membrane pores but does not result in cell death (<a class="reflink" href="/search/result.php?tc=1.A.109#ref34546957">Mart&iacute;n-S&aacute;nchez <em>et al.</em> 2016</a>).</p></div>
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<div class="next-level"><a href="/search/result.php?tc=1.A.109.1">View Proteins belonging to: <span style="color:maroon;">The Interleukin 1 (IL1) Family</span></a></div>
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<h4>References associated with 1.A.109 family:</h4>
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<div class=''>
<A ID="ref34546958"></A>Chojnacka, K., B. Bilinska, and D.D. Mruk. (2016). Interleukin 1α-induced disruption of the Sertoli cell cytoskeleton affects gap junctional communication. Cell Signal 28: 469-480. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=26879129" target="_window">26879129</A></div>
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<div class=''>
<A ID="ref34546959"></A>Martín-Sánchez, F., C. Diamond, M. Zeitler, A.I. Gomez, A. Baroja-Mazo, J. Bagnall, D. Spiller, M. White, M.J. Daniels, A. Mortellaro, M. Peñalver, P. Paszek, J.P. Steringer, W. Nickel, D. Brough, and P. Pelegrín. (2016). Inflammasome-dependent IL-1β release depends upon membrane permeabilisation. Cell Death Differ 23: 1219-1231. <A HREF="http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&term=26868913" target="_window">26868913</A></div>
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