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Phosphorylation‐dependent binding of human transcription factor MOK2 to lamin A/C
Author(s) -
Harper Maryannick,
Tillit Jeanne,
Kress Michel,
ErnoultLange Michèle
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.07032.x
Subject(s) - lamin , phosphorylation , transcription factor , nuclear protein , nuclear matrix , microbiology and biotechnology , biology , kinase , activating transcription factor 2 , protein kinase a , serine , protein phosphorylation , nuclear lamina , dna binding protein , genetics , dna , promoter , gene , chromatin , gene expression , nucleus
Human MOK2 is a DNA‐binding transcriptional repressor. Previously, we identified nuclear lamin A/C proteins as protein partners of hsMOK2. Furthermore, we found that a fraction of hsMOK2 protein was associated with the nuclear matrix. We therefore suggested that hsMOK2 interactions with lamin A/C and the nuclear matrix may be important for its ability to repress transcription. In this study, we identify JNK‐associated leucine zipper and JSAP1 scaffold proteins, two members of c‐Jun N‐terminal kinase (JNK)‐interacting proteins family as partners of hsMOK2. Because these results suggested that hsMOK2 could be phosphorylated, we investigated the phosphorylation status of hsMOK2. We identified Ser38 and Ser129 of hsMOK2 as phosphorylation sites of JNK3 kinase, and Ser46 as a phosphorylation site of Aurora A and protein kinase A. These three serine residues are located in the lamin A/C‐binding domain. Interestingly, we were able to demonstrate that the phosphorylation of hsMOK2 interfered with its ability to bind lamin A/C.