ENTH and ANTH domain proteins participate in AP2-independent clathrin-mediated endocytosis
Identifieur interne : 000112 ( Pmc/Checkpoint ); précédent : 000111; suivant : 000113ENTH and ANTH domain proteins participate in AP2-independent clathrin-mediated endocytosis
Auteurs : Paul T. Manna [Royaume-Uni] ; Catarina Gadelha [Royaume-Uni] ; Amy E. Puttick [Royaume-Uni] ; Mark C. Field [Royaume-Uni]Source :
- Journal of Cell Science [ 0021-9533 ] ; 2015.
Abstract
Clathrin-mediated endocytosis (CME) is a major route of entry into eukaryotic cells. A core of evolutionarily ancient genes encodes many components of this system but much of our mechanistic understanding of CME is derived from a phylogenetically narrow sampling of a few model organisms. In the parasite
Url:
DOI: 10.1242/jcs.167726
PubMed: 25908855
PubMed Central: 4450294
Affiliations:
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">ENTH and ANTH domain proteins participate in AP2-independent clathrin-mediated endocytosis</title>
<author><name sortKey="Manna, Paul T" sort="Manna, Paul T" uniqKey="Manna P" first="Paul T." last="Manna">Paul T. Manna</name>
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<author><name sortKey="Gadelha, Catarina" sort="Gadelha, Catarina" uniqKey="Gadelha C" first="Catarina" last="Gadelha">Catarina Gadelha</name>
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<author><name sortKey="Puttick, Amy E" sort="Puttick, Amy E" uniqKey="Puttick A" first="Amy E." last="Puttick">Amy E. Puttick</name>
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<author><name sortKey="Field, Mark C" sort="Field, Mark C" uniqKey="Field M" first="Mark C." last="Field">Mark C. Field</name>
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<series><title level="j">Journal of Cell Science</title>
<idno type="ISSN">0021-9533</idno>
<idno type="eISSN">1477-9137</idno>
<imprint><date when="2015">2015</date>
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<front><div type="abstract" xml:lang="en"><title>ABSTRACT</title>
<p>Clathrin-mediated endocytosis (CME) is a major route of entry into eukaryotic cells. A core of evolutionarily ancient genes encodes many components of this system but much of our mechanistic understanding of CME is derived from a phylogenetically narrow sampling of a few model organisms. In the parasite <italic>Trypanosoma brucei</italic>
, which is distantly related to the better characterised animals and fungi, exceptionally fast endocytic turnover aids its evasion of the host immune system. Although clathrin is absolutely essential for this process, the adaptor protein complex 2 (AP2) has been secondarily lost, suggesting mechanistic divergence. Here, we characterise two phosphoinositide-binding monomeric clathrin adaptors, <italic>T. brucei</italic>
(Tb)EpsinR and TbCALM, which in trypanosomes are represented by single genes, unlike the expansions present in animals and fungi. Depletion of these gene products reveals essential, but partially redundant, activities in CME. Ultrastructural analysis of TbCALM and TbEpsinR double-knockdown cells demonstrated severe defects to clathrin-coated pit formation and morphology associated with a dramatic inhibition of endocytosis. Depletion of TbCALM alone, however, produced a distinct lysosomal segregation phenotype, indicating an additional non-redundant role for this protein. Therefore, TbEpsinR and TbCALM represent ancient phosphoinositide-binding proteins with distinct and vital roles in AP2-independent endocytosis.</p>
</div>
</front>
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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Cell Sci</journal-id>
<journal-id journal-id-type="iso-abbrev">J. Cell. Sci</journal-id>
<journal-id journal-id-type="publisher-id">JCS</journal-id>
<journal-id journal-id-type="hwp">joces</journal-id>
<journal-title-group><journal-title>Journal of Cell Science</journal-title>
</journal-title-group>
<issn pub-type="ppub">0021-9533</issn>
<issn pub-type="epub">1477-9137</issn>
<publisher><publisher-name>The Company of Biologists</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">25908855</article-id>
<article-id pub-id-type="pmc">4450294</article-id>
<article-id pub-id-type="doi">10.1242/jcs.167726</article-id>
<article-id pub-id-type="publisher-id">JCS167726</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>ENTH and ANTH domain proteins participate in AP2-independent clathrin-mediated endocytosis</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Manna</surname>
<given-names>Paul T.</given-names>
</name>
<xref ref-type="aff" rid="af1">1</xref>
<xref ref-type="author-notes" rid="AN1">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Gadelha</surname>
<given-names>Catarina</given-names>
</name>
<xref ref-type="aff" rid="af2">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Puttick</surname>
<given-names>Amy E.</given-names>
</name>
<xref ref-type="aff" rid="af1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Field</surname>
<given-names>Mark C.</given-names>
</name>
<xref ref-type="aff" rid="af3">3</xref>
<xref ref-type="corresp" rid="cor1">‡</xref>
</contrib>
</contrib-group>
<aff id="af1"><label>1</label>
<institution>Department of Pathology, University of Cambridge</institution>
,<addr-line>Tennis Court Road, Cambridge CB2 1QP</addr-line>
,<country>UK</country>
</aff>
<aff id="af2"><label>2</label>
<institution>School of Life Sciences, University of Nottingham</institution>
,<addr-line>Queen's Medical Centre, Nottingham NG7 2UH</addr-line>
,<country>UK</country>
</aff>
<aff id="af3"><label>3</label>
<institution>Division of Biological Chemistry and Drug Discovery, University of Dundee</institution>
,<addr-line>Dundee DD1 5EH</addr-line>
,<country>UK</country>
</aff>
<author-notes><fn id="AN1"><label>*</label>
<p>Present address: Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, UK.</p>
</fn>
<corresp id="cor1"><label>‡</label>
Author for correspondence (<email>m.c.field@dundee.ac.uk</email>
)</corresp>
</author-notes>
<pub-date pub-type="ppub"><day>1</day>
<month>6</month>
<year>2015</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>1</day>
<month>6</month>
<year>2015</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
. </pmc-comment>
<volume>128</volume>
<issue>11</issue>
<fpage>2130</fpage>
<lpage>2142</lpage>
<history><date date-type="received"><day>16</day>
<month>12</month>
<year>2014</year>
</date>
<date date-type="accepted"><day>13</day>
<month>4</month>
<year>2015</year>
</date>
</history>
<permissions><copyright-statement>© 2015. Published by The Company of Biologists Ltd</copyright-statement>
<copyright-year>2015</copyright-year>
<license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/3.0"><license-p>This is an Open Access article distributed under the terms of the Creative Commons Attribution License (<uri xlink:href="http://creativecommons.org/licenses/by/3.0">http://creativecommons.org/licenses/by/3.0</uri>
), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.</license-p>
</license>
</permissions>
<self-uri content-type="pdf" xlink:href="JCS167726.pdf"></self-uri>
<abstract><title>ABSTRACT</title>
<p>Clathrin-mediated endocytosis (CME) is a major route of entry into eukaryotic cells. A core of evolutionarily ancient genes encodes many components of this system but much of our mechanistic understanding of CME is derived from a phylogenetically narrow sampling of a few model organisms. In the parasite <italic>Trypanosoma brucei</italic>
, which is distantly related to the better characterised animals and fungi, exceptionally fast endocytic turnover aids its evasion of the host immune system. Although clathrin is absolutely essential for this process, the adaptor protein complex 2 (AP2) has been secondarily lost, suggesting mechanistic divergence. Here, we characterise two phosphoinositide-binding monomeric clathrin adaptors, <italic>T. brucei</italic>
(Tb)EpsinR and TbCALM, which in trypanosomes are represented by single genes, unlike the expansions present in animals and fungi. Depletion of these gene products reveals essential, but partially redundant, activities in CME. Ultrastructural analysis of TbCALM and TbEpsinR double-knockdown cells demonstrated severe defects to clathrin-coated pit formation and morphology associated with a dramatic inhibition of endocytosis. Depletion of TbCALM alone, however, produced a distinct lysosomal segregation phenotype, indicating an additional non-redundant role for this protein. Therefore, TbEpsinR and TbCALM represent ancient phosphoinositide-binding proteins with distinct and vital roles in AP2-independent endocytosis.</p>
</abstract>
<kwd-group><title>KEY WORDS</title>
<kwd>Endocytosis</kwd>
<kwd>Evolution</kwd>
<kwd>Phosphoinositide</kwd>
<kwd>Trafficking</kwd>
<kwd>Trypanosome</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>Royaume-Uni</li>
</country>
</list>
<tree><country name="Royaume-Uni"><noRegion><name sortKey="Manna, Paul T" sort="Manna, Paul T" uniqKey="Manna P" first="Paul T." last="Manna">Paul T. Manna</name>
</noRegion>
<name sortKey="Field, Mark C" sort="Field, Mark C" uniqKey="Field M" first="Mark C." last="Field">Mark C. Field</name>
<name sortKey="Gadelha, Catarina" sort="Gadelha, Catarina" uniqKey="Gadelha C" first="Catarina" last="Gadelha">Catarina Gadelha</name>
<name sortKey="Puttick, Amy E" sort="Puttick, Amy E" uniqKey="Puttick A" first="Amy E." last="Puttick">Amy E. Puttick</name>
</country>
</tree>
</affiliations>
</record>
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