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The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM
Centrosomes comprise a pair of centrioles surrounded by a matrix of pericentriolar material (PCM). In vertebrate cells, Pericentrin plays an important part in mitotic PCM assembly, but the Drosophila Pericentrin-like protein (PLP) appears to have a more minor role in mitotic fly cells. Here we inves...
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Published in: | Biology open 2015-08, Vol.4 (8), p.1052-1061 |
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description | Centrosomes comprise a pair of centrioles surrounded by a matrix of pericentriolar material (PCM). In vertebrate cells, Pericentrin plays an important part in mitotic PCM assembly, but the Drosophila Pericentrin-like protein (PLP) appears to have a more minor role in mitotic fly cells. Here we investigate the function of PLP during the rapid mitotic cycles of the early Drosophila embryo. Unexpectedly, we find that PLP is specifically enriched in the outer-most regions of the PCM, where it largely co-localizes with the PCM scaffold protein Cnn. In the absence of PLP the outer PCM appears to be structurally weakened, and it rapidly disperses along the centrosomal microtubules (MTs). As a result, centrosomal MTs are subtly disorganized in embryos lacking PLP, although mitosis is largely unperturbed and these embryos develop and hatch at near-normal rates. Y2H analysis reveals that PLP can potentially form multiple interactions with itself and with the PCM recruiting proteins Asl, Spd-2 and Cnn. A deletion analysis suggests that PLP participates in a complex network of interactions that ultimately help to strengthen the PCM. |
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In vertebrate cells, Pericentrin plays an important part in mitotic PCM assembly, but the Drosophila Pericentrin-like protein (PLP) appears to have a more minor role in mitotic fly cells. Here we investigate the function of PLP during the rapid mitotic cycles of the early Drosophila embryo. Unexpectedly, we find that PLP is specifically enriched in the outer-most regions of the PCM, where it largely co-localizes with the PCM scaffold protein Cnn. In the absence of PLP the outer PCM appears to be structurally weakened, and it rapidly disperses along the centrosomal microtubules (MTs). As a result, centrosomal MTs are subtly disorganized in embryos lacking PLP, although mitosis is largely unperturbed and these embryos develop and hatch at near-normal rates. Y2H analysis reveals that PLP can potentially form multiple interactions with itself and with the PCM recruiting proteins Asl, Spd-2 and Cnn. A deletion analysis suggests that PLP participates in a complex network of interactions that ultimately help to strengthen the PCM.</description><identifier>ISSN: 2046-6390</identifier><identifier>EISSN: 2046-6390</identifier><identifier>DOI: 10.1242/bio.012914</identifier><identifier>PMID: 26157019</identifier><language>eng</language><publisher>England: The Company of Biologists Ltd</publisher><subject>Centriole ; Centrioles ; Centrosome ; Centrosomes ; Drosophila ; Embryos ; Fruit flies ; Insects ; Microtubules ; Mitosis ; PCM ; Pericentrin ; Proteins ; Spindle ; Vertebrates</subject><ispartof>Biology open, 2015-08, Vol.4 (8), p.1052-1061</ispartof><rights>2015. Published by The Company of Biologists Ltd.</rights><rights>2015. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015. Published by The Company of Biologists Ltd 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c575t-2434c47fa8947455130aeaef9077f5b6f3cd3e56dd007b790c188deadc6f89d83</citedby><cites>FETCH-LOGICAL-c575t-2434c47fa8947455130aeaef9077f5b6f3cd3e56dd007b790c188deadc6f89d83</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/PMC4542290/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2761068841?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26157019$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Richens, Jennifer H</creatorcontrib><creatorcontrib>Barros, Teresa P</creatorcontrib><creatorcontrib>Lucas, Eliana P</creatorcontrib><creatorcontrib>Peel, Nina</creatorcontrib><creatorcontrib>Pinto, David Miguel Susano</creatorcontrib><creatorcontrib>Wainman, Alan</creatorcontrib><creatorcontrib>Raff, Jordan W</creatorcontrib><title>The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM</title><title>Biology open</title><addtitle>Biol Open</addtitle><description>Centrosomes comprise a pair of centrioles surrounded by a matrix of pericentriolar material (PCM). 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In vertebrate cells, Pericentrin plays an important part in mitotic PCM assembly, but the Drosophila Pericentrin-like protein (PLP) appears to have a more minor role in mitotic fly cells. Here we investigate the function of PLP during the rapid mitotic cycles of the early Drosophila embryo. Unexpectedly, we find that PLP is specifically enriched in the outer-most regions of the PCM, where it largely co-localizes with the PCM scaffold protein Cnn. In the absence of PLP the outer PCM appears to be structurally weakened, and it rapidly disperses along the centrosomal microtubules (MTs). As a result, centrosomal MTs are subtly disorganized in embryos lacking PLP, although mitosis is largely unperturbed and these embryos develop and hatch at near-normal rates. Y2H analysis reveals that PLP can potentially form multiple interactions with itself and with the PCM recruiting proteins Asl, Spd-2 and Cnn. A deletion analysis suggests that PLP participates in a complex network of interactions that ultimately help to strengthen the PCM.</abstract><cop>England</cop><pub>The Company of Biologists Ltd</pub><pmid>26157019</pmid><doi>10.1242/bio.012914</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Centriole Centrioles Centrosome Centrosomes Drosophila Embryos Fruit flies Insects Microtubules Mitosis PCM Pericentrin Proteins Spindle Vertebrates |
title | The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM |
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