The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.

Lamins' functions are regulated by phosphorylation at specific sites but our understanding of the role of such modifications is practically limited to the function of cdc 2 (cdk1) kinase sites in depolymerization of the nuclear lamina during mitosis. In our study we used Drosophila lamin Dm (B-...

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Autores principales:	Magdalena Zaremba-Czogalla, Katarzyna Piekarowicz, Katarzyna Wachowicz, Katarzyna Kozioł, Magda Dubińska-Magiera, Ryszard Rzepecki
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e42e09c0a1624f0ebcb24604c0eec1e7
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spelling	oai:doaj.org-article:e42e09c0a1624f0ebcb24604c0eec1e72021-11-18T07:26:22ZThe different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.1932-620310.1371/journal.pone.0032649https://doaj.org/article/e42e09c0a1624f0ebcb24604c0eec1e72012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22393432/?tool=EBIhttps://doaj.org/toc/1932-6203Lamins' functions are regulated by phosphorylation at specific sites but our understanding of the role of such modifications is practically limited to the function of cdc 2 (cdk1) kinase sites in depolymerization of the nuclear lamina during mitosis. In our study we used Drosophila lamin Dm (B-type) to examine the function of particular phosphorylation sites using pseudophosphorylated mutants mimicking single phosphorylation at experimentally confirmed in vivo phosphosites (S(25)E, S(45)E, T(435)E, S(595)E). We also analyzed lamin C (A-type) and its mutant S(37)E representing the N-terminal cdc2 (mitotic) site as well as lamin Dm R(64)H mutant as a control, non-polymerizing lamin. In the polymerization assay we could observe different effects of N-terminal cdc2 site pseudophosphorylation on A- and B-type lamins: lamin Dm S(45)E mutant was insoluble, in contrast to lamin C S(37)E. Lamin Dm T(435)E (C-terminal cdc2 site) and R(64)H were soluble in vitro. We also confirmed that none of the single phosphorylation site modifications affected the chromatin binding of lamin Dm, in contrast to the lamin C N-terminal cdc2 site. In vivo, all lamin Dm mutants were incorporated efficiently into the nuclear lamina in transfected Drosophila S2 and HeLa cells, although significant amounts of S(45)E and T(435)E were also located in cytoplasm. When farnesylation incompetent mutants were expressed in HeLa cells, lamin Dm T(435)E was cytoplasmic and showed higher mobility in FRAP assay.Magdalena Zaremba-CzogallaKatarzyna PiekarowiczKatarzyna WachowiczKatarzyna KoziołMagda Dubińska-MagieraRyszard RzepeckiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 2, p e32649 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Magdalena Zaremba-Czogalla Katarzyna Piekarowicz Katarzyna Wachowicz Katarzyna Kozioł Magda Dubińska-Magiera Ryszard Rzepecki The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.
description	Lamins' functions are regulated by phosphorylation at specific sites but our understanding of the role of such modifications is practically limited to the function of cdc 2 (cdk1) kinase sites in depolymerization of the nuclear lamina during mitosis. In our study we used Drosophila lamin Dm (B-type) to examine the function of particular phosphorylation sites using pseudophosphorylated mutants mimicking single phosphorylation at experimentally confirmed in vivo phosphosites (S(25)E, S(45)E, T(435)E, S(595)E). We also analyzed lamin C (A-type) and its mutant S(37)E representing the N-terminal cdc2 (mitotic) site as well as lamin Dm R(64)H mutant as a control, non-polymerizing lamin. In the polymerization assay we could observe different effects of N-terminal cdc2 site pseudophosphorylation on A- and B-type lamins: lamin Dm S(45)E mutant was insoluble, in contrast to lamin C S(37)E. Lamin Dm T(435)E (C-terminal cdc2 site) and R(64)H were soluble in vitro. We also confirmed that none of the single phosphorylation site modifications affected the chromatin binding of lamin Dm, in contrast to the lamin C N-terminal cdc2 site. In vivo, all lamin Dm mutants were incorporated efficiently into the nuclear lamina in transfected Drosophila S2 and HeLa cells, although significant amounts of S(45)E and T(435)E were also located in cytoplasm. When farnesylation incompetent mutants were expressed in HeLa cells, lamin Dm T(435)E was cytoplasmic and showed higher mobility in FRAP assay.
format	article
author	Magdalena Zaremba-Czogalla Katarzyna Piekarowicz Katarzyna Wachowicz Katarzyna Kozioł Magda Dubińska-Magiera Ryszard Rzepecki
author_facet	Magdalena Zaremba-Czogalla Katarzyna Piekarowicz Katarzyna Wachowicz Katarzyna Kozioł Magda Dubińska-Magiera Ryszard Rzepecki
author_sort	Magdalena Zaremba-Czogalla
title	The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.
title_short	The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.
title_full	The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.
title_fullStr	The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.
title_full_unstemmed	The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.
title_sort	different function of single phosphorylation sites of drosophila melanogaster lamin dm and lamin c.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/e42e09c0a1624f0ebcb24604c0eec1e7
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The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.

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