The role of myosin 1c and myosin 1b in surfactant exocytosis
Actin and actin-associated proteins have a pivotal effect on regulated exocytosis in secretory cells and influence pre-fusion as well as post-fusion stages of exocytosis. Actin polymerization on secretory granules during the post-fusion phase (formation of an actin coat) is especially important in c...
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| Veröffentlicht in: | Journal of cell science 2016-04, Vol.129 (8), p.1685-1696 |
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| container_issue | 8 |
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| container_title | Journal of cell science |
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| creator | Kittelberger, Nadine Breunig, Markus Martin, René Knölker, Hans-Joachim Miklavc, Pika |
| description | Actin and actin-associated proteins have a pivotal effect on regulated exocytosis in secretory cells and influence pre-fusion as well as post-fusion stages of exocytosis. Actin polymerization on secretory granules during the post-fusion phase (formation of an actin coat) is especially important in cells with large secretory vesicles or poorly soluble secretions. Alveolar type II (ATII) cells secrete hydrophobic lipo-protein surfactant, which does not easily diffuse from fused vesicles. Previous work showed that compression of actin coat is necessary for surfactant extrusion. Here, we investigate the role of class 1 myosins as possible linkers between actin and membranes during exocytosis. Live-cell microscopy showed translocation of fluorescently labeled myosin 1b and myosin 1c to the secretory vesicle membrane after fusion. Myosin 1c translocation was dependent on its pleckstrin homology domain. Expression of myosin 1b and myosin 1c constructs influenced vesicle compression rate, whereas only the inhibition of myosin 1c reduced exocytosis. These findings suggest that class 1 myosins participate in several stages of ATII cell exocytosis and link actin coats to the secretory vesicle membrane to influence vesicle compression. |
| doi_str_mv | 10.1242/jcs.181313 |
| format | Article |
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Actin polymerization on secretory granules during the post-fusion phase (formation of an actin coat) is especially important in cells with large secretory vesicles or poorly soluble secretions. Alveolar type II (ATII) cells secrete hydrophobic lipo-protein surfactant, which does not easily diffuse from fused vesicles. Previous work showed that compression of actin coat is necessary for surfactant extrusion. Here, we investigate the role of class 1 myosins as possible linkers between actin and membranes during exocytosis. Live-cell microscopy showed translocation of fluorescently labeled myosin 1b and myosin 1c to the secretory vesicle membrane after fusion. Myosin 1c translocation was dependent on its pleckstrin homology domain. Expression of myosin 1b and myosin 1c constructs influenced vesicle compression rate, whereas only the inhibition of myosin 1c reduced exocytosis. 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Actin polymerization on secretory granules during the post-fusion phase (formation of an actin coat) is especially important in cells with large secretory vesicles or poorly soluble secretions. Alveolar type II (ATII) cells secrete hydrophobic lipo-protein surfactant, which does not easily diffuse from fused vesicles. Previous work showed that compression of actin coat is necessary for surfactant extrusion. Here, we investigate the role of class 1 myosins as possible linkers between actin and membranes during exocytosis. Live-cell microscopy showed translocation of fluorescently labeled myosin 1b and myosin 1c to the secretory vesicle membrane after fusion. Myosin 1c translocation was dependent on its pleckstrin homology domain. Expression of myosin 1b and myosin 1c constructs influenced vesicle compression rate, whereas only the inhibition of myosin 1c reduced exocytosis. These findings suggest that class 1 myosins participate in several stages of ATII cell exocytosis and link actin coats to the secretory vesicle membrane to influence vesicle compression.</description><subject>Actin Cytoskeleton - metabolism</subject><subject>Alveolar Epithelial Cells - physiology</subject><subject>Animals</subject><subject>Bodily Secretions</subject><subject>Cells, Cultured</subject><subject>Exocytosis - genetics</subject><subject>Male</subject><subject>Membrane Fusion - genetics</subject><subject>Myosin Type I - genetics</subject><subject>Myosin Type I - metabolism</subject><subject>Pulmonary Surfactants - metabolism</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Secretory Vesicles - physiology</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkFtLw0AQhRdRbK2--AMkjyJEd3Y22SyIIMUbFHypz8tmLzYlzdZsIvbfG2kt-jLDzPk4MxxCzoFeA-PsZmniNRSAgAdkDFyIVAKKQzKmlEEqM8QROYlxSSkVTIpjMmK55FSCGJPb-cIlbahdEnyy2oRYNQmYRDd2P5XJUGPfem063XSJ-wpm0w1aPCVHXtfRne36hLw9Psynz-ns9ellej9LDYqiS0EzaWxmmWQIVFieSVNKLg1D43XpLaPgCxBIHXowOWQSLKIddpIjzXFC7ra-675cOWtc07W6Vuu2Wul2o4Ku1H-lqRbqPXwqXmRM5HIwuNwZtOGjd7FTqyoaV9e6caGPCkQBGUfM-YBebVHThhhb5_dngKqfuNUQt9rGPcAXfx_bo7_54jffpnqE</recordid><startdate>20160415</startdate><enddate>20160415</enddate><creator>Kittelberger, Nadine</creator><creator>Breunig, Markus</creator><creator>Martin, René</creator><creator>Knölker, Hans-Joachim</creator><creator>Miklavc, Pika</creator><general>The Company of Biologists Ltd</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160415</creationdate><title>The role of myosin 1c and myosin 1b in surfactant exocytosis</title><author>Kittelberger, Nadine ; Breunig, Markus ; Martin, René ; Knölker, Hans-Joachim ; Miklavc, Pika</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-1a29cd5d2923107d459cb949c23cfabfd201f81730e3f1c61591d33df81943063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Actin Cytoskeleton - metabolism</topic><topic>Alveolar Epithelial Cells - physiology</topic><topic>Animals</topic><topic>Bodily Secretions</topic><topic>Cells, Cultured</topic><topic>Exocytosis - genetics</topic><topic>Male</topic><topic>Membrane Fusion - genetics</topic><topic>Myosin Type I - genetics</topic><topic>Myosin Type I - metabolism</topic><topic>Pulmonary Surfactants - metabolism</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Secretory Vesicles - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kittelberger, Nadine</creatorcontrib><creatorcontrib>Breunig, Markus</creatorcontrib><creatorcontrib>Martin, René</creatorcontrib><creatorcontrib>Knölker, Hans-Joachim</creatorcontrib><creatorcontrib>Miklavc, Pika</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kittelberger, Nadine</au><au>Breunig, Markus</au><au>Martin, René</au><au>Knölker, Hans-Joachim</au><au>Miklavc, Pika</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of myosin 1c and myosin 1b in surfactant exocytosis</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2016-04-15</date><risdate>2016</risdate><volume>129</volume><issue>8</issue><spage>1685</spage><epage>1696</epage><pages>1685-1696</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>Actin and actin-associated proteins have a pivotal effect on regulated exocytosis in secretory cells and influence pre-fusion as well as post-fusion stages of exocytosis. Actin polymerization on secretory granules during the post-fusion phase (formation of an actin coat) is especially important in cells with large secretory vesicles or poorly soluble secretions. Alveolar type II (ATII) cells secrete hydrophobic lipo-protein surfactant, which does not easily diffuse from fused vesicles. Previous work showed that compression of actin coat is necessary for surfactant extrusion. Here, we investigate the role of class 1 myosins as possible linkers between actin and membranes during exocytosis. Live-cell microscopy showed translocation of fluorescently labeled myosin 1b and myosin 1c to the secretory vesicle membrane after fusion. Myosin 1c translocation was dependent on its pleckstrin homology domain. Expression of myosin 1b and myosin 1c constructs influenced vesicle compression rate, whereas only the inhibition of myosin 1c reduced exocytosis. 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| ispartof | Journal of cell science, 2016-04, Vol.129 (8), p.1685-1696 |
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| subjects | Actin Cytoskeleton - metabolism Alveolar Epithelial Cells - physiology Animals Bodily Secretions Cells, Cultured Exocytosis - genetics Male Membrane Fusion - genetics Myosin Type I - genetics Myosin Type I - metabolism Pulmonary Surfactants - metabolism Rats Rats, Sprague-Dawley Secretory Vesicles - physiology |
| title | The role of myosin 1c and myosin 1b in surfactant exocytosis |
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