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Page 1
Microfilament dynamics: regulation of actin polymerization by actin-fragmin kinase and phosphatases.
Waelkens E, Gettemans J, De Corte V, De Ville Y, Goris J, Vandekerckhove J, Merlevede W. Waelkens E, et al. Among authors: de corte v. Adv Enzyme Regul. 1995;35:199-227. doi: 10.1016/0065-2571(94)00013-s. Adv Enzyme Regul. 1995. PMID: 7572344 Review.
This kinase phosphorylates the actin moiety of the actin-fragmin complex at two consecutive threonine residues which constitute one of the contact sites for DNase I (37) and which are also located at one of the proposed actin-actin contact sites along the long-pitch helix of F …
This kinase phosphorylates the actin moiety of the actin-fragmin complex at two consecutive threonine residues which constitute one of the c …
Marine microbial metagenomes sampled across space and time.
Biller SJ, Berube PM, Dooley K, Williams M, Satinsky BM, Hackl T, Hogle SL, Coe A, Bergauer K, Bouman HA, Browning TJ, De Corte D, Hassler C, Hulston D, Jacquot JE, Maas EW, Reinthaler T, Sintes E, Yokokawa T, Chisholm SW. Biller SJ, et al. Among authors: de corte d. Sci Data. 2018 Sep 4;5:180176. doi: 10.1038/sdata.2018.176. Sci Data. 2018. PMID: 30179232 Free PMC article.
A novel endogenous PP2C-like phosphatase dephosphorylates casein kinase II-phosphorylated Physarum fragmin.
Waelkens E, de Corte V, Merlevede W, Vandekerckhove J, Gettemans J. Waelkens E, et al. Among authors: de corte v. Biochem Biophys Res Commun. 2000 Dec 20;279(2):438-44. doi: 10.1006/bbrc.2000.3990. Biochem Biophys Res Commun. 2000. PMID: 11118305
Plasmodial fragmin, a Physarum polycephalum F-actin severing and capping protein, is phosphorylated by casein kinase II at Ser(266) (De Corte, V., Gettemans, J., De Ville, Y., Waelkens, E., and Vandekerckchove, J. (1996), Biochemistry 35, 5472-5480). ...
Plasmodial fragmin, a Physarum polycephalum F-actin severing and capping protein, is phosphorylated by casein kinase II at Ser(266) ( …
A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction.
Van den Abbeele A, De Clercq S, De Ganck A, De Corte V, Van Loo B, Soror SH, Srinivasan V, Steyaert J, Vandekerckhove J, Gettemans J. Van den Abbeele A, et al. Among authors: de corte v. Cell Mol Life Sci. 2010 May;67(9):1519-35. doi: 10.1007/s00018-010-0266-1. Epub 2010 Feb 7. Cell Mol Life Sci. 2010. PMID: 20140750 Free PMC article.
Both GsnVHHs trace gelsolin in membrane ruffles of EGF-stimulated MCF-7 cells and delay cell migration without affecting F-actin severing/capping or actin nucleation activities by gelsolin. We conclude that VHHs represent a potent way of blocking structural proteins and th …
Both GsnVHHs trace gelsolin in membrane ruffles of EGF-stimulated MCF-7 cells and delay cell migration without affecting F-actin seve …
Fragmin, a microfilament regulatory protein from Physarum polycephalum, is phosphorylated by casein kinase II-type enzymes.
De Corte V, Gettemans J, De Ville Y, Waelkens E, Vandekerckhove J. De Corte V, et al. Biochemistry. 1996 Apr 30;35(17):5472-80. doi: 10.1021/bi952237r. Biochemistry. 1996. PMID: 8611538
Interestingly, the actin-fragmin dimer (A--F) as well as the actin2-fragmin trimer (A2--F) are equally efficient targets, and phosphorylation had no effect on the actin-binding properties of fragmin. ...
Interestingly, the actin-fragmin dimer (A--F) as well as the actin2-fragmin trimer (A2--F) are equally efficient targets, and …
The Nucleo-cytoplasmic actin-binding protein CapG lacks a nuclear export sequence present in structurally related proteins.
Van Impe K, De Corte V, Eichinger L, Bruyneel E, Mareel M, Vandekerckhove J, Gettemans J. Van Impe K, et al. Among authors: de corte v. J Biol Chem. 2003 May 16;278(20):17945-52. doi: 10.1074/jbc.M209946200. Epub 2003 Mar 11. J Biol Chem. 2003. PMID: 12637565 Free article.
Despite thorough structure-function analyses, it remains unclear how CapG, a ubiquitous F-actin barbed end capping protein that controls actin microfilament turnover in cells, is able to reside in the nucleus and cytoplasm, whereas structurally related actin-binding protei …
Despite thorough structure-function analyses, it remains unclear how CapG, a ubiquitous F-actin barbed end capping protein that contr …
Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells.
Janji B, Giganti A, De Corte V, Catillon M, Bruyneel E, Lentz D, Plastino J, Gettemans J, Friederich E. Janji B, et al. Among authors: de corte v. J Cell Sci. 2006 May 1;119(Pt 9):1947-60. doi: 10.1242/jcs.02874. J Cell Sci. 2006. PMID: 16636079
Conversely, a Ser5Glu variant mimicking a constitutively phosphorylated state, accumulated in actin-rich regions and promoted the formation of F-actin microspikes in two cell lines. Similar to phosphorylated wild-type L-plastin, this variant remained associated with cellul …
Conversely, a Ser5Glu variant mimicking a constitutively phosphorylated state, accumulated in actin-rich regions and promoted the formation …
In vivo phosphorylation of actin in Physarum polycephalum. Study of the substrate specificity of the actin-fragmin kinase.
De Corte V, Gettemans J, Waelkens E, Vandekerckhove J. De Corte V, et al. Eur J Biochem. 1996 Nov 1;241(3):901-8. doi: 10.1111/j.1432-1033.1996.00901.x. Eur J Biochem. 1996. PMID: 8944781 Free article.
Actin-fragmin is a heterodimeric protein complex from Physarum polycephalum microplasmodia that is phosphorylated in vitro at residues Thr203 and Thr202 of the actin subunit by the endogenous actin-fragmin kinase. Following phosphorylation, the F-actin capping activity of …
Actin-fragmin is a heterodimeric protein complex from Physarum polycephalum microplasmodia that is phosphorylated in vitro at residues Thr20 …
Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid.
Meerschaert K, De Corte V, De Ville Y, Vandekerckhove J, Gettemans J. Meerschaert K, et al. Among authors: de corte v. EMBO J. 1998 Oct 15;17(20):5923-32. doi: 10.1093/emboj/17.20.5923. EMBO J. 1998. PMID: 9774337 Free PMC article.
We found that the structurally simplest lysophospholipid, lysophosphatidic acid (LPA), dissociated the complex between fragminP and actin, whereas other lysophospholipids or sphingosine-1-phosphate were inactive. Furthermore, LPA inhibited the F-actin severing activity of …
We found that the structurally simplest lysophospholipid, lysophosphatidic acid (LPA), dissociated the complex between fragminP and actin, w …
Single cell genomes of Prochlorococcus, Synechococcus, and sympatric microbes from diverse marine environments.
Berube PM, Biller SJ, Hackl T, Hogle SL, Satinsky BM, Becker JW, Braakman R, Collins SB, Kelly L, Berta-Thompson J, Coe A, Bergauer K, Bouman HA, Browning TJ, De Corte D, Hassler C, Hulata Y, Jacquot JE, Maas EW, Reinthaler T, Sintes E, Yokokawa T, Lindell D, Stepanauskas R, Chisholm SW. Berube PM, et al. Among authors: de corte d. Sci Data. 2018 Sep 4;5:180154. doi: 10.1038/sdata.2018.154. Sci Data. 2018. PMID: 30179231 Free PMC article.
15 results