Chemotaxis: signalling modules join hands at front and tail
Chemotaxis is the result of a refined interplay among various intracellular molecules that process spatial and temporal information. Here we present a modular scheme of the complex interactions between the front and the back of cells that allows them to navigate. First, at the front of the cell, act...
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| Veröffentlicht in: | EMBO reports 2004-01, Vol.5 (1), p.35-40 |
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| creator | Postma, Marten Bosgraaf, Leonard Loovers, Harriët M Van Haastert, Peter J M |
| description | Chemotaxis is the result of a refined interplay among various intracellular molecules that process spatial and temporal information. Here we present a modular scheme of the complex interactions between the front and the back of cells that allows them to navigate. First, at the front of the cell, activated Rho‐type GTPases induce actin polymerization and pseudopod formation. Second, phosphatidylinositol‐3,4,5‐trisphosphate (PtdIns(3,4,5)P
3
) is produced in a patch at the leading edge, where it binds pleckstrin‐homology‐domain‐containing proteins, which enhance actin polymerization and translocation of the pseudopod. Third, in
Dictyostelium
amoebae, a cyclic‐GMP‐signalling cascade has been identified that regulates myosin filament formation in the posterior of the cell, thereby inhibiting the formation of lateral pseudopodia that could misdirect the cell. |
| doi_str_mv | 10.1038/sj.embor.7400051 |
| format | Article |
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3
) is produced in a patch at the leading edge, where it binds pleckstrin‐homology‐domain‐containing proteins, which enhance actin polymerization and translocation of the pseudopod. Third, in
Dictyostelium
amoebae, a cyclic‐GMP‐signalling cascade has been identified that regulates myosin filament formation in the posterior of the cell, thereby inhibiting the formation of lateral pseudopodia that could misdirect the cell.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>EISSN: 1469-221X</identifier><identifier>DOI: 10.1038/sj.embor.7400051</identifier><identifier>PMID: 14710184</identifier><identifier>CODEN: ERMEAX</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>5)P3 ; actin ; Animals ; Cell Shape ; cGMP ; Chemotaxis ; Concept ; Cyclic GMP - metabolism ; Dictyostelium ; Dictyostelium - cytology ; Dictyostelium - physiology ; modules ; myosin ; Phosphatidylinositol Phosphates - metabolism ; Pseudopodia - metabolism ; Pseudopodia - physiology ; PtdIns ; PtdIns(3,4,5)P3 ; Review ; Signal Transduction ; Translocation</subject><ispartof>EMBO reports, 2004-01, Vol.5 (1), p.35-40</ispartof><rights>European Molecular Biology Organization 2004</rights><rights>Copyright © 2004 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Jan 2004</rights><rights>Copyright © 2004, European Molecular Biology Organization 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5801-8be1c37c43d9e144fdfe8be191e8d54c38c0a77ba5748b8dd2a71b7eb116d5703</citedby><cites>FETCH-LOGICAL-c5801-8be1c37c43d9e144fdfe8be191e8d54c38c0a77ba5748b8dd2a71b7eb116d5703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1298962/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1298962/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14710184$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Postma, Marten</creatorcontrib><creatorcontrib>Bosgraaf, Leonard</creatorcontrib><creatorcontrib>Loovers, Harriët M</creatorcontrib><creatorcontrib>Van Haastert, Peter J M</creatorcontrib><title>Chemotaxis: signalling modules join hands at front and tail</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>Chemotaxis is the result of a refined interplay among various intracellular molecules that process spatial and temporal information. Here we present a modular scheme of the complex interactions between the front and the back of cells that allows them to navigate. First, at the front of the cell, activated Rho‐type GTPases induce actin polymerization and pseudopod formation. Second, phosphatidylinositol‐3,4,5‐trisphosphate (PtdIns(3,4,5)P
3
) is produced in a patch at the leading edge, where it binds pleckstrin‐homology‐domain‐containing proteins, which enhance actin polymerization and translocation of the pseudopod. Third, in
Dictyostelium
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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Postma, Marten</au><au>Bosgraaf, Leonard</au><au>Loovers, Harriët M</au><au>Van Haastert, Peter J M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chemotaxis: signalling modules join hands at front and tail</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2004-01</date><risdate>2004</risdate><volume>5</volume><issue>1</issue><spage>35</spage><epage>40</epage><pages>35-40</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><eissn>1469-221X</eissn><coden>ERMEAX</coden><abstract>Chemotaxis is the result of a refined interplay among various intracellular molecules that process spatial and temporal information. Here we present a modular scheme of the complex interactions between the front and the back of cells that allows them to navigate. First, at the front of the cell, activated Rho‐type GTPases induce actin polymerization and pseudopod formation. Second, phosphatidylinositol‐3,4,5‐trisphosphate (PtdIns(3,4,5)P
3
) is produced in a patch at the leading edge, where it binds pleckstrin‐homology‐domain‐containing proteins, which enhance actin polymerization and translocation of the pseudopod. Third, in
Dictyostelium
amoebae, a cyclic‐GMP‐signalling cascade has been identified that regulates myosin filament formation in the posterior of the cell, thereby inhibiting the formation of lateral pseudopodia that could misdirect the cell.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>14710184</pmid><doi>10.1038/sj.embor.7400051</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | 5)P3 actin Animals Cell Shape cGMP Chemotaxis Concept Cyclic GMP - metabolism Dictyostelium Dictyostelium - cytology Dictyostelium - physiology modules myosin Phosphatidylinositol Phosphates - metabolism Pseudopodia - metabolism Pseudopodia - physiology PtdIns PtdIns(3,4,5)P3 Review Signal Transduction Translocation |
| title | Chemotaxis: signalling modules join hands at front and tail |
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