Connexin/Innexin Channels in Cytoplasmic Organelles. Are There Intracellular Gap Junctions? A Hypothesis
This paper proposes the hypothesis that cytoplasmic organelles directly interact with each other and with gap junctions forming intracellular junctions. This hypothesis originated over four decades ago based on the observation that vesicles lining gap junctions of crayfish giant axons contain electr...
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| Veröffentlicht in: | International journal of molecular sciences 2020-03, Vol.21 (6), p.2163, Article 2163 |
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| description | This paper proposes the hypothesis that cytoplasmic organelles directly interact with each other and with gap junctions forming intracellular junctions. This hypothesis originated over four decades ago based on the observation that vesicles lining gap junctions of crayfish giant axons contain electron-opaque particles, similar in size to junctional innexons that often appear to directly interact with junctional innexons; similar particles were seen also in the outer membrane of crayfish mitochondria. Indeed, vertebrate connexins assembled into hexameric connexons are present not only in the membranes of the Golgi apparatus but also in those of the mitochondria and endoplasmic reticulum. It seems possible, therefore, that cytoplasmic organelles may be able to exchange small molecules with each other as well as with organelles of coupled cells via gap junctions. |
| doi_str_mv | 10.3390/ijms21062163 |
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This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). 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Are There Intracellular Gap Junctions? A Hypothesis</title><title>International journal of molecular sciences</title><addtitle>INT J MOL SCI</addtitle><addtitle>Int J Mol Sci</addtitle><description>This paper proposes the hypothesis that cytoplasmic organelles directly interact with each other and with gap junctions forming intracellular junctions. This hypothesis originated over four decades ago based on the observation that vesicles lining gap junctions of crayfish giant axons contain electron-opaque particles, similar in size to junctional innexons that often appear to directly interact with junctional innexons; similar particles were seen also in the outer membrane of crayfish mitochondria. Indeed, vertebrate connexins assembled into hexameric connexons are present not only in the membranes of the Golgi apparatus but also in those of the mitochondria and endoplasmic reticulum. It seems possible, therefore, that cytoplasmic organelles may be able to exchange small molecules with each other as well as with organelles of coupled cells via gap junctions.</description><subject>Animals</subject><subject>Astacoidea</subject><subject>Axons</subject><subject>Axons - metabolism</subject><subject>Axons - ultrastructure</subject><subject>Binding sites</subject><subject>Biochemistry & Molecular Biology</subject><subject>Biological Transport - physiology</subject><subject>calmodulin</subject><subject>Calmodulin - chemistry</subject><subject>Calmodulin - metabolism</subject><subject>cell-to-cell channels</subject><subject>channel gating</subject><subject>Chemistry</subject><subject>Chemistry, Multidisciplinary</subject><subject>Communication</subject><subject>connexin</subject><subject>Connexins</subject><subject>Connexins - chemistry</subject><subject>Connexins - metabolism</subject><subject>Crayfish</subject><subject>crayfish giant axons</subject><subject>Cytoplasm - metabolism</subject><subject>Cytoplasmic Vesicles - metabolism</subject><subject>Cytoplasmic Vesicles - ultrastructure</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Gap junctions</subject><subject>Gap Junctions - metabolism</subject><subject>Gap Junctions - ultrastructure</subject><subject>Giant axons</subject><subject>Golgi apparatus</subject><subject>Golgi Apparatus - metabolism</subject><subject>Hypotheses</subject><subject>Hypothesis</subject><subject>innexin</subject><subject>Intracellular</subject><subject>Ion Channels - metabolism</subject><subject>Life Sciences & Biomedicine</subject><subject>liver</subject><subject>Membranes</subject><subject>Microscopy, Electron</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitochondria - ultrastructure</subject><subject>Models, Chemical</subject><subject>Organelles</subject><subject>Physical Sciences</subject><subject>Plasma</subject><subject>Science & Technology</subject><subject>stomach</subject><subject>Submitochondrial Particles - metabolism</subject><subject>Submitochondrial Particles - ultrastructure</subject><subject>Vertebrates</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>AOWDO</sourceid><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><sourceid>DOA</sourceid><recordid>eNqNkk1v1DAQhiMEoqVw44wicUGCbe2x4yQX0CqCdlGlXsrZmjiTXa-y8WInwP57HFJWW05cPKPxo1fz8SbJa84uhSjZld3uAnCmgCvxJDnnEmDBmMqfnuRnyYsQtoyBgKx8npwJAJnxojxPNpXre_pl-6vVHNNqgzHrQjrlh8HtOww7a9I7v8ZY7yhcpktP6f2G4rvqB48mlscOfXqN-_Tr2JvBuj58SpfpzWHvhg0FG14mz1rsAr16iBfJty-f76ubxe3d9apa3i6MzIthkbVcEeOyzHOTS24KzIllddkStNAW1AAZAKqxIcgF51K2JTYmQ1TYKMjERbKadRuHW733dof-oB1a_afg_FqjH6zpSIOSDcuwqDNZSyhE3SpCyRm0jCQCRK2Ps9Z-rHfUGJqG7R6JPv7p7Uav3Q-dcxEHmJp59yDg3feRwqB3Nkzbipt0Y9AgCgUF5EpF9O0_6NaNvo-rmigBkxyL1IeZMt6F4Kk9NsOZnuygT-0Q8TenAxzhv_ePwPsZ-Em1a4Ox1Bs6YoyxDMqiZBCtk0108f90ZQecfFC5sR_Eb09h0mY</recordid><startdate>20200321</startdate><enddate>20200321</enddate><creator>Peracchia, Camillo</creator><general>Mdpi</general><general>MDPI AG</general><general>MDPI</general><scope>AOWDO</scope><scope>BLEPL</scope><scope>DTL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0001-7405-1271</orcidid></search><sort><creationdate>20200321</creationdate><title>Connexin/Innexin Channels in Cytoplasmic Organelles. 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Are There Intracellular Gap Junctions? A Hypothesis</atitle><jtitle>International journal of molecular sciences</jtitle><stitle>INT J MOL SCI</stitle><addtitle>Int J Mol Sci</addtitle><date>2020-03-21</date><risdate>2020</risdate><volume>21</volume><issue>6</issue><spage>2163</spage><pages>2163-</pages><artnum>2163</artnum><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>This paper proposes the hypothesis that cytoplasmic organelles directly interact with each other and with gap junctions forming intracellular junctions. This hypothesis originated over four decades ago based on the observation that vesicles lining gap junctions of crayfish giant axons contain electron-opaque particles, similar in size to junctional innexons that often appear to directly interact with junctional innexons; similar particles were seen also in the outer membrane of crayfish mitochondria. Indeed, vertebrate connexins assembled into hexameric connexons are present not only in the membranes of the Golgi apparatus but also in those of the mitochondria and endoplasmic reticulum. It seems possible, therefore, that cytoplasmic organelles may be able to exchange small molecules with each other as well as with organelles of coupled cells via gap junctions.</abstract><cop>BASEL</cop><pub>Mdpi</pub><pmid>32245189</pmid><doi>10.3390/ijms21062163</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-7405-1271</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Astacoidea Axons Axons - metabolism Axons - ultrastructure Binding sites Biochemistry & Molecular Biology Biological Transport - physiology calmodulin Calmodulin - chemistry Calmodulin - metabolism cell-to-cell channels channel gating Chemistry Chemistry, Multidisciplinary Communication connexin Connexins Connexins - chemistry Connexins - metabolism Crayfish crayfish giant axons Cytoplasm - metabolism Cytoplasmic Vesicles - metabolism Cytoplasmic Vesicles - ultrastructure Endoplasmic reticulum Endoplasmic Reticulum - metabolism Gap junctions Gap Junctions - metabolism Gap Junctions - ultrastructure Giant axons Golgi apparatus Golgi Apparatus - metabolism Hypotheses Hypothesis innexin Intracellular Ion Channels - metabolism Life Sciences & Biomedicine liver Membranes Microscopy, Electron Mitochondria Mitochondria - metabolism Mitochondria - ultrastructure Models, Chemical Organelles Physical Sciences Plasma Science & Technology stomach Submitochondrial Particles - metabolism Submitochondrial Particles - ultrastructure Vertebrates |
| title | Connexin/Innexin Channels in Cytoplasmic Organelles. Are There Intracellular Gap Junctions? A Hypothesis |
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