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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003793naa a2200385 4500
001oai:DiVA.org:uu-115540
003SwePub
008100217s2010 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:119901519
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-1155402 URI
0247 a https://doi.org/10.1091/mbc.E09-06-05042 DOI
0247 a http://kipublications.ki.se/Default.aspx?queryparsed=id:1199015192 URI
040 a (SwePub)uud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a MacPherson, Matthew Reidu Departamento de Bioquímica, UAM, Instituto de Investigaciones Biome´dicas “Alberto Sols,” CSIC-UAM, 28029 Madrid, Spain4 aut
2451 0a Phosphorylation of serine 11 and serine 92 as new positive regulators of human Snail1 function :b potential involvement of casein kinase-2 and the cAMP-activated kinase protein kinase A
264 1c 2010
338 a print2 rdacarrier
520 a Snail1 is a major factor for epithelial-mesenchymal transition (EMT), an important event in tumor metastasis and in other pathologies. Snail1 is tightly regulated at transcriptional and posttranscriptional levels. Control of Snail1 protein stability and nuclear export by GSK3beta phosphorylation is important for Snail1 functionality. Stabilization mechanisms independent of GSK3beta have also been reported, including interaction with LOXL2 or regulation of the COP9 signalosome by inflammatory signals. To get further insights into the role of Snail1 phosphorylation, we have performed an in-depth analysis of in vivo human Snail1 phosphorylation combined with mutational studies. We identify new phosphorylation sites at serines 11, 82, and 92 and confirmed previously suggested phosphorylations at serine 104 and 107. Serines 11 and 92 participate in the control of Snail1 stability and positively regulate Snail1 repressive function and its interaction with mSin3A corepressor. Furthermore, serines 11 and 92 are required for Snail1-mediated EMT and cell viability, respectively. PKA and CK2 have been characterized as the main kinases responsible for in vitro Snail1 phosphorylation at serine 11 and 92, respectively. These results highlight serines 11 and 92 as new players in Snail1 regulation and suggest the participation of CK2 and PKA in the modulation of Snail1 functionality.
653 a MEDICINE
653 a MEDICIN
7001 a Molina, Patriciau Departamento de Bioquímica, UAM, Instituto de Investigaciones Biome´dicas “Alberto Sols,” CSIC-UAM, 28029 Madrid, Spain4 aut
7001 a Souchelnytskyi, Serhiyu Karolinska Institutet4 aut
7001 a Wernstedt, Christeru Uppsala universitet,Ludwiginstitutet för cancerforskning4 aut0 (Swepub:uu)chrisws
7001 a Martin-Pérez, Jorgeu Departamento de Bioquímica, UAM, Instituto de Investigaciones Biome´dicas “Alberto Sols,” CSIC-UAM, 28029 Madrid, Spain4 aut
7001 a Portillo, Franciscou Departamento de Bioquímica, UAM, Instituto de Investigaciones Biome´dicas “Alberto Sols,” CSIC-UAM, 28029 Madrid, Spain4 aut
7001 a Cano, Amparou Departamento de Bioquímica, UAM, Instituto de Investigaciones Biome´dicas “Alberto Sols,” CSIC-UAM, 28029 Madrid, Spain4 aut
7102 a Karolinska Institutetb Departamento de Bioquímica, UAM, Instituto de Investigaciones Biome´dicas “Alberto Sols,” CSIC-UAM, 28029 Madrid, Spain4 org
7730 t Molecular Biology of the Cellg 21:2, s. 244-253q 21:2<244-253x 1059-1524x 1939-4586
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-115540
8564 8u https://doi.org/10.1091/mbc.E09-06-0504
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:119901519

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