Spatiotemporal distribution of PKCα, Cdc42, and Rac1 before directed cell migration
Cdc42 is a key factor in directed cell migration and accumulates at the leading edge of migrating cells. However, what kind of proteins control Cdc42 and when is unclear. After mechanical wounding, protein kinase C α (PKCα), a conventional PKC isozyme, begins to accumulate at the edges of cells adja...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2021-12, Vol.584, p.26-31 |
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| creator | Sasaki, Saori Takahashi, Ryu Luo, Yangfeng Chujo, Kengo Sera, Toshihiro Kudo, Susumu |
| description | Cdc42 is a key factor in directed cell migration and accumulates at the leading edge of migrating cells. However, what kind of proteins control Cdc42 and when is unclear. After mechanical wounding, protein kinase C α (PKCα), a conventional PKC isozyme, begins to accumulate at the edges of cells adjacent to the wounded cells (WCs). In this study, we hypothesized that PKCα may be implicated in directed cell migration at an early stage before Cdc42 controls the migration. We focused on the spatiotemporal distribution of PKCα, Cdc42, and Rac1 before cell migration. After wounding, at the edges of cells adjacent to the WCs, PKCα accumulation, Cdc42 accumulation, Rac1 accumulation, and filopodia formation occurred in that order. The PKCα inhibitor suppressed Cdc42 accumulation at the cell edges. These results suggest that inhibition of PKCα activity inhibits cell migration. In addition, it is not Cdc42 but PKCα that may decide the direction of cell migration.
•PKCα accumulates at edge of cells faster than Cdc42 after mechanical wounding.•PKCα controls Cdc42 and directed cell migration.•PKCα, not Cdc42, is a trigger for directed cell migration after mechanical wounding. |
| doi_str_mv | 10.1016/j.bbrc.2021.10.080 |
| format | Article |
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•PKCα accumulates at edge of cells faster than Cdc42 after mechanical wounding.•PKCα controls Cdc42 and directed cell migration.•PKCα, not Cdc42, is a trigger for directed cell migration after mechanical wounding.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2021.10.080</identifier><identifier>PMID: 34753065</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Bryostatins - pharmacology ; Calcium - metabolism ; Cdc42 ; cdc42 GTP-Binding Protein - genetics ; cdc42 GTP-Binding Protein - metabolism ; Cell migration ; Cell Movement ; Cells, Cultured ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; Intracellular Space - drug effects ; Intracellular Space - metabolism ; Keratinocytes - cytology ; Keratinocytes - metabolism ; Microscopy, Fluorescence - methods ; Protein Kinase C-alpha - genetics ; Protein Kinase C-alpha - metabolism ; Protein kinase Cα ; Rac1 ; rac1 GTP-Binding Protein - genetics ; rac1 GTP-Binding Protein - metabolism ; Rats ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Stress, Mechanical ; Time-Lapse Imaging - methods</subject><ispartof>Biochemical and biophysical research communications, 2021-12, Vol.584, p.26-31</ispartof><rights>2021 Elsevier Inc.</rights><rights>Copyright © 2021 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3150-14d28e6a908c32a7521e7a1e19ceabdac36561fbe7ca61bdc6541fe5eae3c8e33</citedby><cites>FETCH-LOGICAL-c3150-14d28e6a908c32a7521e7a1e19ceabdac36561fbe7ca61bdc6541fe5eae3c8e33</cites><orcidid>0000-0001-6241-8005 ; 0000-0003-0782-2309</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X21015047$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34753065$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sasaki, Saori</creatorcontrib><creatorcontrib>Takahashi, Ryu</creatorcontrib><creatorcontrib>Luo, Yangfeng</creatorcontrib><creatorcontrib>Chujo, Kengo</creatorcontrib><creatorcontrib>Sera, Toshihiro</creatorcontrib><creatorcontrib>Kudo, Susumu</creatorcontrib><title>Spatiotemporal distribution of PKCα, Cdc42, and Rac1 before directed cell migration</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Cdc42 is a key factor in directed cell migration and accumulates at the leading edge of migrating cells. However, what kind of proteins control Cdc42 and when is unclear. After mechanical wounding, protein kinase C α (PKCα), a conventional PKC isozyme, begins to accumulate at the edges of cells adjacent to the wounded cells (WCs). In this study, we hypothesized that PKCα may be implicated in directed cell migration at an early stage before Cdc42 controls the migration. We focused on the spatiotemporal distribution of PKCα, Cdc42, and Rac1 before cell migration. After wounding, at the edges of cells adjacent to the WCs, PKCα accumulation, Cdc42 accumulation, Rac1 accumulation, and filopodia formation occurred in that order. The PKCα inhibitor suppressed Cdc42 accumulation at the cell edges. These results suggest that inhibition of PKCα activity inhibits cell migration. In addition, it is not Cdc42 but PKCα that may decide the direction of cell migration.
•PKCα accumulates at edge of cells faster than Cdc42 after mechanical wounding.•PKCα controls Cdc42 and directed cell migration.•PKCα, not Cdc42, is a trigger for directed cell migration after mechanical wounding.</description><subject>Animals</subject><subject>Bryostatins - pharmacology</subject><subject>Calcium - metabolism</subject><subject>Cdc42</subject><subject>cdc42 GTP-Binding Protein - genetics</subject><subject>cdc42 GTP-Binding Protein - metabolism</subject><subject>Cell migration</subject><subject>Cell Movement</subject><subject>Cells, Cultured</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>Intracellular Space - drug effects</subject><subject>Intracellular Space - metabolism</subject><subject>Keratinocytes - cytology</subject><subject>Keratinocytes - metabolism</subject><subject>Microscopy, Fluorescence - methods</subject><subject>Protein Kinase C-alpha - genetics</subject><subject>Protein Kinase C-alpha - metabolism</subject><subject>Protein kinase Cα</subject><subject>Rac1</subject><subject>rac1 GTP-Binding Protein - genetics</subject><subject>rac1 GTP-Binding Protein - metabolism</subject><subject>Rats</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Stress, Mechanical</subject><subject>Time-Lapse Imaging - methods</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kNtKxDAQhoMouh5ewAvJpRd2nUmbbAveyOIJBcUDeBfSZCpZtu2adAUfyxfxmWzZ1UuvBn6--Zn5GDtEGCOgOp2NyzLYsQCBfTCGHDbYCKGARCBkm2wEACoRBb7usN0YZwCImSq22U6aTWQKSo7Y89PCdL7tqF60wcy587ELvlz2WcPbij_cTr-_TvjU2UyccNM4_mgs8pKqNlBPB7IdOW5pPue1fwtDWbPPtiozj3Swnnvs5fLieXqd3N1f3UzP7xKbooQEMydyUqaA3KbCTKRAmhgkLCyZ0hmbKqmwKmlijcLSWSUzrEiSodTmlKZ77HjVuwjt-5Jip2sfh1NMQ-0yaiELBSilzHtUrFAb2hgDVXoRfG3Cp0bQg00904NNPdgcst5mv3S07l-WNbm_lV99PXC2Aqj_8sNT0NF6aiytxGjX-v_6fwCiX4YX</recordid><startdate>20211220</startdate><enddate>20211220</enddate><creator>Sasaki, Saori</creator><creator>Takahashi, Ryu</creator><creator>Luo, Yangfeng</creator><creator>Chujo, Kengo</creator><creator>Sera, Toshihiro</creator><creator>Kudo, Susumu</creator><general>Elsevier Inc</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><orcidid>https://orcid.org/0000-0001-6241-8005</orcidid><orcidid>https://orcid.org/0000-0003-0782-2309</orcidid></search><sort><creationdate>20211220</creationdate><title>Spatiotemporal distribution of PKCα, Cdc42, and Rac1 before directed cell migration</title><author>Sasaki, Saori ; Takahashi, Ryu ; Luo, Yangfeng ; Chujo, Kengo ; Sera, Toshihiro ; Kudo, Susumu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3150-14d28e6a908c32a7521e7a1e19ceabdac36561fbe7ca61bdc6541fe5eae3c8e33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Animals</topic><topic>Bryostatins - pharmacology</topic><topic>Calcium - metabolism</topic><topic>Cdc42</topic><topic>cdc42 GTP-Binding Protein - genetics</topic><topic>cdc42 GTP-Binding Protein - metabolism</topic><topic>Cell migration</topic><topic>Cell Movement</topic><topic>Cells, Cultured</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>Intracellular Space - drug effects</topic><topic>Intracellular Space - metabolism</topic><topic>Keratinocytes - cytology</topic><topic>Keratinocytes - metabolism</topic><topic>Microscopy, Fluorescence - methods</topic><topic>Protein Kinase C-alpha - genetics</topic><topic>Protein Kinase C-alpha - metabolism</topic><topic>Protein kinase Cα</topic><topic>Rac1</topic><topic>rac1 GTP-Binding Protein - genetics</topic><topic>rac1 GTP-Binding Protein - metabolism</topic><topic>Rats</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Stress, Mechanical</topic><topic>Time-Lapse Imaging - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sasaki, Saori</creatorcontrib><creatorcontrib>Takahashi, Ryu</creatorcontrib><creatorcontrib>Luo, Yangfeng</creatorcontrib><creatorcontrib>Chujo, Kengo</creatorcontrib><creatorcontrib>Sera, Toshihiro</creatorcontrib><creatorcontrib>Kudo, Susumu</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><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sasaki, Saori</au><au>Takahashi, Ryu</au><au>Luo, Yangfeng</au><au>Chujo, Kengo</au><au>Sera, Toshihiro</au><au>Kudo, Susumu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Spatiotemporal distribution of PKCα, Cdc42, and Rac1 before directed cell migration</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2021-12-20</date><risdate>2021</risdate><volume>584</volume><spage>26</spage><epage>31</epage><pages>26-31</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Cdc42 is a key factor in directed cell migration and accumulates at the leading edge of migrating cells. However, what kind of proteins control Cdc42 and when is unclear. After mechanical wounding, protein kinase C α (PKCα), a conventional PKC isozyme, begins to accumulate at the edges of cells adjacent to the wounded cells (WCs). In this study, we hypothesized that PKCα may be implicated in directed cell migration at an early stage before Cdc42 controls the migration. We focused on the spatiotemporal distribution of PKCα, Cdc42, and Rac1 before cell migration. After wounding, at the edges of cells adjacent to the WCs, PKCα accumulation, Cdc42 accumulation, Rac1 accumulation, and filopodia formation occurred in that order. The PKCα inhibitor suppressed Cdc42 accumulation at the cell edges. These results suggest that inhibition of PKCα activity inhibits cell migration. In addition, it is not Cdc42 but PKCα that may decide the direction of cell migration.
•PKCα accumulates at edge of cells faster than Cdc42 after mechanical wounding.•PKCα controls Cdc42 and directed cell migration.•PKCα, not Cdc42, is a trigger for directed cell migration after mechanical wounding.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>34753065</pmid><doi>10.1016/j.bbrc.2021.10.080</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0001-6241-8005</orcidid><orcidid>https://orcid.org/0000-0003-0782-2309</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Bryostatins - pharmacology Calcium - metabolism Cdc42 cdc42 GTP-Binding Protein - genetics cdc42 GTP-Binding Protein - metabolism Cell migration Cell Movement Cells, Cultured Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism Intracellular Space - drug effects Intracellular Space - metabolism Keratinocytes - cytology Keratinocytes - metabolism Microscopy, Fluorescence - methods Protein Kinase C-alpha - genetics Protein Kinase C-alpha - metabolism Protein kinase Cα Rac1 rac1 GTP-Binding Protein - genetics rac1 GTP-Binding Protein - metabolism Rats Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Stress, Mechanical Time-Lapse Imaging - methods |
| title | Spatiotemporal distribution of PKCα, Cdc42, and Rac1 before directed cell migration |
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