Loss of the Dictyostelium RasC protein alters vegetative cell size, motility and endocytosis
In addition to its previously established roles in cAMP relay and cAMP chemotaxis, loss of signal transduction through the RasC protein was found to impact a number of vegetative cell functions. Vegetative rasC − cells exhibited reduced random motility, were less polarized and had altered F-actin di...
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| Veröffentlicht in: | Experimental cell research 2005-05, Vol.306 (1), p.47-55 |
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| creator | Lim, Chinten James Zawadzki, Karl A. Khosla, Meenal Secko, David M. Spiegelman, George B. Weeks, Gerald |
| description | In addition to its previously established roles in cAMP relay and cAMP chemotaxis, loss of signal transduction through the RasC protein was found to impact a number of vegetative cell functions. Vegetative
rasC
−
cells exhibited reduced random motility, were less polarized and had altered F-actin distribution. Cells lacking RasC also contained more protein and were larger in size than wild type cells. These increases were associated with increased liquid phase endocytosis. Despite the increase in cell size, cytokinesis was relatively normal and there was no change in the rate of cell division.
rasC
−
cells also chemotaxed poorly to folate and exhibited reduced F-actin accumulation, reduced ERK2 phosphorylation and reduced Akt/PKB phosphorylation in response to folate, indicating that RasC was also involved in transducing chemotactic signals in vegetative cells. |
| doi_str_mv | 10.1016/j.yexcr.2005.02.002 |
| format | Article |
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rasC
−
cells exhibited reduced random motility, were less polarized and had altered F-actin distribution. Cells lacking RasC also contained more protein and were larger in size than wild type cells. These increases were associated with increased liquid phase endocytosis. Despite the increase in cell size, cytokinesis was relatively normal and there was no change in the rate of cell division.
rasC
−
cells also chemotaxed poorly to folate and exhibited reduced F-actin accumulation, reduced ERK2 phosphorylation and reduced Akt/PKB phosphorylation in response to folate, indicating that RasC was also involved in transducing chemotactic signals in vegetative cells.</description><identifier>ISSN: 0014-4827</identifier><identifier>EISSN: 1090-2422</identifier><identifier>DOI: 10.1016/j.yexcr.2005.02.002</identifier><identifier>PMID: 15878331</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>3-Phosphoinositide-Dependent Protein Kinases ; Actins - metabolism ; Akt/PKB ; Animals ; Cell Division - genetics ; Cell Division - physiology ; Cell size ; Chemotaxis - genetics ; Chemotaxis - physiology ; Cytoskeleton ; Dextrans - metabolism ; Dictyostelium - cytology ; Dictyostelium - physiology ; Endocytosis ; Endocytosis - genetics ; Endocytosis - physiology ; ERK2 ; Fluorescein-5-isothiocyanate - analogs & derivatives ; Fluorescein-5-isothiocyanate - metabolism ; Folate ; Folic Acid - metabolism ; MAP Kinase Kinase 2 - metabolism ; Motility ; Phosphorylation ; Pinocytosis - genetics ; Pinocytosis - physiology ; Protein-Serine-Threonine Kinases - metabolism ; Protozoan Proteins - genetics ; Protozoan Proteins - physiology ; Ras ; ras Proteins - deficiency ; ras Proteins - genetics ; ras Proteins - physiology ; Signal Transduction - physiology</subject><ispartof>Experimental cell research, 2005-05, Vol.306 (1), p.47-55</ispartof><rights>2005 Elsevier Inc.</rights><rights>Copyright © 2005 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c384t-c8226ec83b1cd1349ca860bbc83d4ad71ba9aea9abeec0af7ceacfb9b6301e7d3</citedby><cites>FETCH-LOGICAL-c384t-c8226ec83b1cd1349ca860bbc83d4ad71ba9aea9abeec0af7ceacfb9b6301e7d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.yexcr.2005.02.002$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3554,27933,27934,46004</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15878331$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lim, Chinten James</creatorcontrib><creatorcontrib>Zawadzki, Karl A.</creatorcontrib><creatorcontrib>Khosla, Meenal</creatorcontrib><creatorcontrib>Secko, David M.</creatorcontrib><creatorcontrib>Spiegelman, George B.</creatorcontrib><creatorcontrib>Weeks, Gerald</creatorcontrib><title>Loss of the Dictyostelium RasC protein alters vegetative cell size, motility and endocytosis</title><title>Experimental cell research</title><addtitle>Exp Cell Res</addtitle><description>In addition to its previously established roles in cAMP relay and cAMP chemotaxis, loss of signal transduction through the RasC protein was found to impact a number of vegetative cell functions. Vegetative
rasC
−
cells exhibited reduced random motility, were less polarized and had altered F-actin distribution. Cells lacking RasC also contained more protein and were larger in size than wild type cells. These increases were associated with increased liquid phase endocytosis. Despite the increase in cell size, cytokinesis was relatively normal and there was no change in the rate of cell division.
rasC
−
cells also chemotaxed poorly to folate and exhibited reduced F-actin accumulation, reduced ERK2 phosphorylation and reduced Akt/PKB phosphorylation in response to folate, indicating that RasC was also involved in transducing chemotactic signals in vegetative cells.</description><subject>3-Phosphoinositide-Dependent Protein Kinases</subject><subject>Actins - metabolism</subject><subject>Akt/PKB</subject><subject>Animals</subject><subject>Cell Division - genetics</subject><subject>Cell Division - physiology</subject><subject>Cell size</subject><subject>Chemotaxis - genetics</subject><subject>Chemotaxis - physiology</subject><subject>Cytoskeleton</subject><subject>Dextrans - metabolism</subject><subject>Dictyostelium - cytology</subject><subject>Dictyostelium - physiology</subject><subject>Endocytosis</subject><subject>Endocytosis - genetics</subject><subject>Endocytosis - physiology</subject><subject>ERK2</subject><subject>Fluorescein-5-isothiocyanate - analogs & derivatives</subject><subject>Fluorescein-5-isothiocyanate - metabolism</subject><subject>Folate</subject><subject>Folic Acid - metabolism</subject><subject>MAP Kinase Kinase 2 - metabolism</subject><subject>Motility</subject><subject>Phosphorylation</subject><subject>Pinocytosis - genetics</subject><subject>Pinocytosis - physiology</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Protozoan Proteins - genetics</subject><subject>Protozoan Proteins - physiology</subject><subject>Ras</subject><subject>ras Proteins - deficiency</subject><subject>ras Proteins - genetics</subject><subject>ras Proteins - physiology</subject><subject>Signal Transduction - physiology</subject><issn>0014-4827</issn><issn>1090-2422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1r3DAQhkVJ6W62_QWFInLIKXZHsteWDz2E7VdgoVDaW0HI0jjRYltbSV7i_vpquwuFHHIYBoZnZl4eQt4yyBmw6v0un_FR-5wDrHPgOQB_QZYMGsh4yfkFWQKwMisFrxfkMoQdAAjBqldkwdaiFkXBluTX1oVAXUfjA9KPVsfZhYi9nQb6XYUN3XsX0Y5U9RF9oAe8x6iiPSDV2Pc02D94QwcXbW_jTNVoKI7G6Tm6YMNr8rJTfcA3574iPz9_-rH5mm2_fbnb3G4zXYgyZlpwXqEWRcu0YUXZaCUqaNs0MaUyNWtVozBVi6hBdbVGpbu2aasCGNamWJHr092U9veEIcrBhmM-NaKbgqxqkYQxkcCrJ-DOTX5M2SRrymrN15wnqDhB2ic3Hju593ZQfpYM5NG83Ml_5uXRvAQuk_m09e58emoHNP93zqoT8OEEYDJxsOhl0BZHjcZ61FEaZ5998Bf-NJfr</recordid><startdate>20050515</startdate><enddate>20050515</enddate><creator>Lim, Chinten James</creator><creator>Zawadzki, Karl A.</creator><creator>Khosla, Meenal</creator><creator>Secko, David M.</creator><creator>Spiegelman, George B.</creator><creator>Weeks, Gerald</creator><general>Elsevier Inc</general><general>Elsevier BV</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>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20050515</creationdate><title>Loss of the Dictyostelium RasC protein alters vegetative cell size, motility and endocytosis</title><author>Lim, Chinten James ; Zawadzki, Karl A. ; Khosla, Meenal ; Secko, David M. ; Spiegelman, George B. ; Weeks, Gerald</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c384t-c8226ec83b1cd1349ca860bbc83d4ad71ba9aea9abeec0af7ceacfb9b6301e7d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>3-Phosphoinositide-Dependent Protein Kinases</topic><topic>Actins - metabolism</topic><topic>Akt/PKB</topic><topic>Animals</topic><topic>Cell Division - genetics</topic><topic>Cell Division - physiology</topic><topic>Cell size</topic><topic>Chemotaxis - genetics</topic><topic>Chemotaxis - physiology</topic><topic>Cytoskeleton</topic><topic>Dextrans - metabolism</topic><topic>Dictyostelium - cytology</topic><topic>Dictyostelium - physiology</topic><topic>Endocytosis</topic><topic>Endocytosis - genetics</topic><topic>Endocytosis - physiology</topic><topic>ERK2</topic><topic>Fluorescein-5-isothiocyanate - analogs & derivatives</topic><topic>Fluorescein-5-isothiocyanate - metabolism</topic><topic>Folate</topic><topic>Folic Acid - metabolism</topic><topic>MAP Kinase Kinase 2 - metabolism</topic><topic>Motility</topic><topic>Phosphorylation</topic><topic>Pinocytosis - genetics</topic><topic>Pinocytosis - physiology</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Protozoan Proteins - genetics</topic><topic>Protozoan Proteins - physiology</topic><topic>Ras</topic><topic>ras Proteins - deficiency</topic><topic>ras Proteins - genetics</topic><topic>ras Proteins - physiology</topic><topic>Signal Transduction - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lim, Chinten James</creatorcontrib><creatorcontrib>Zawadzki, Karl A.</creatorcontrib><creatorcontrib>Khosla, Meenal</creatorcontrib><creatorcontrib>Secko, David M.</creatorcontrib><creatorcontrib>Spiegelman, George B.</creatorcontrib><creatorcontrib>Weeks, Gerald</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Experimental cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lim, Chinten James</au><au>Zawadzki, Karl A.</au><au>Khosla, Meenal</au><au>Secko, David M.</au><au>Spiegelman, George B.</au><au>Weeks, Gerald</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Loss of the Dictyostelium RasC protein alters vegetative cell size, motility and endocytosis</atitle><jtitle>Experimental cell research</jtitle><addtitle>Exp Cell Res</addtitle><date>2005-05-15</date><risdate>2005</risdate><volume>306</volume><issue>1</issue><spage>47</spage><epage>55</epage><pages>47-55</pages><issn>0014-4827</issn><eissn>1090-2422</eissn><abstract>In addition to its previously established roles in cAMP relay and cAMP chemotaxis, loss of signal transduction through the RasC protein was found to impact a number of vegetative cell functions. Vegetative
rasC
−
cells exhibited reduced random motility, were less polarized and had altered F-actin distribution. Cells lacking RasC also contained more protein and were larger in size than wild type cells. These increases were associated with increased liquid phase endocytosis. Despite the increase in cell size, cytokinesis was relatively normal and there was no change in the rate of cell division.
rasC
−
cells also chemotaxed poorly to folate and exhibited reduced F-actin accumulation, reduced ERK2 phosphorylation and reduced Akt/PKB phosphorylation in response to folate, indicating that RasC was also involved in transducing chemotactic signals in vegetative cells.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15878331</pmid><doi>10.1016/j.yexcr.2005.02.002</doi><tpages>9</tpages></addata></record> |
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| subjects | 3-Phosphoinositide-Dependent Protein Kinases Actins - metabolism Akt/PKB Animals Cell Division - genetics Cell Division - physiology Cell size Chemotaxis - genetics Chemotaxis - physiology Cytoskeleton Dextrans - metabolism Dictyostelium - cytology Dictyostelium - physiology Endocytosis Endocytosis - genetics Endocytosis - physiology ERK2 Fluorescein-5-isothiocyanate - analogs & derivatives Fluorescein-5-isothiocyanate - metabolism Folate Folic Acid - metabolism MAP Kinase Kinase 2 - metabolism Motility Phosphorylation Pinocytosis - genetics Pinocytosis - physiology Protein-Serine-Threonine Kinases - metabolism Protozoan Proteins - genetics Protozoan Proteins - physiology Ras ras Proteins - deficiency ras Proteins - genetics ras Proteins - physiology Signal Transduction - physiology |
| title | Loss of the Dictyostelium RasC protein alters vegetative cell size, motility and endocytosis |
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