Cargando…
Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis
Cell morphogenesis is a complex process that relies on a diverse array of proteins and pathways. We have identified a transglutaminase-like protein (Cyk3p) that functions in fission yeast morphogenesis. The phenotype of a cyk3 knockout strain indicates a primary role for Cyk3p in cytokinesis. Corres...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3386208/ https://www.ncbi.nlm.nih.gov/pubmed/22573890 http://dx.doi.org/10.1091/mbc.E11-07-0656 |
_version_ | 1782236947564986368 |
---|---|
author | Pollard, Luther W. Onishi, Masayuki Pringle, John R. Lord, Matthew |
author_facet | Pollard, Luther W. Onishi, Masayuki Pringle, John R. Lord, Matthew |
author_sort | Pollard, Luther W. |
collection | PubMed |
description | Cell morphogenesis is a complex process that relies on a diverse array of proteins and pathways. We have identified a transglutaminase-like protein (Cyk3p) that functions in fission yeast morphogenesis. The phenotype of a cyk3 knockout strain indicates a primary role for Cyk3p in cytokinesis. Correspondingly, Cyk3p localizes both to the actomyosin contractile ring and the division septum, promoting ring constriction, septation, and subsequent cell separation following ring disassembly. In addition, Cyk3p localizes to polarized growth sites and plays a role in cell shape determination, and it also appears to contribute to cell integrity during stationary phase, given its accumulation as dynamic puncta at the cortex of such cells. Our results and the conservation of Cyk3p across fungi point to a role in cell wall synthesis and remodeling. Cyk3p possesses a transglutaminase domain that is essential for function, even though it lacks the catalytic active site. In a wider sense, our work illustrates the physiological importance of inactive members of the transglutaminase family, which are found throughout eukaryotes. We suggest that the proposed evolution of animal transglutaminase cross-linking activity from ancestral bacterial thiol proteases was accompanied by the emergence of a subclass whose function does not depend on enzymatic activity. |
format | Online Article Text |
id | pubmed-3386208 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-33862082012-09-16 Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis Pollard, Luther W. Onishi, Masayuki Pringle, John R. Lord, Matthew Mol Biol Cell Articles Cell morphogenesis is a complex process that relies on a diverse array of proteins and pathways. We have identified a transglutaminase-like protein (Cyk3p) that functions in fission yeast morphogenesis. The phenotype of a cyk3 knockout strain indicates a primary role for Cyk3p in cytokinesis. Correspondingly, Cyk3p localizes both to the actomyosin contractile ring and the division septum, promoting ring constriction, septation, and subsequent cell separation following ring disassembly. In addition, Cyk3p localizes to polarized growth sites and plays a role in cell shape determination, and it also appears to contribute to cell integrity during stationary phase, given its accumulation as dynamic puncta at the cortex of such cells. Our results and the conservation of Cyk3p across fungi point to a role in cell wall synthesis and remodeling. Cyk3p possesses a transglutaminase domain that is essential for function, even though it lacks the catalytic active site. In a wider sense, our work illustrates the physiological importance of inactive members of the transglutaminase family, which are found throughout eukaryotes. We suggest that the proposed evolution of animal transglutaminase cross-linking activity from ancestral bacterial thiol proteases was accompanied by the emergence of a subclass whose function does not depend on enzymatic activity. The American Society for Cell Biology 2012-07-01 /pmc/articles/PMC3386208/ /pubmed/22573890 http://dx.doi.org/10.1091/mbc.E11-07-0656 Text en © 2012 Pollard et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Pollard, Luther W. Onishi, Masayuki Pringle, John R. Lord, Matthew Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis |
title | Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis |
title_full | Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis |
title_fullStr | Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis |
title_full_unstemmed | Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis |
title_short | Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis |
title_sort | fission yeast cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3386208/ https://www.ncbi.nlm.nih.gov/pubmed/22573890 http://dx.doi.org/10.1091/mbc.E11-07-0656 |
work_keys_str_mv | AT pollardlutherw fissionyeastcyk3pisatransglutaminaselikeproteinthatparticipatesincytokinesisandcellmorphogenesis AT onishimasayuki fissionyeastcyk3pisatransglutaminaselikeproteinthatparticipatesincytokinesisandcellmorphogenesis AT pringlejohnr fissionyeastcyk3pisatransglutaminaselikeproteinthatparticipatesincytokinesisandcellmorphogenesis AT lordmatthew fissionyeastcyk3pisatransglutaminaselikeproteinthatparticipatesincytokinesisandcellmorphogenesis |