FEZ1 Dimerization and Interaction with Transcription Regulatory Proteins Involves Its Coiled-coil Region Export

@article{citeulike:1560346, abstract = {The fasciculation and elongation protein {zeta}1 (FEZ1) is a mammalian orthologue of the Caenorhabditis elegans protein UNC-76, which is necessary for axon growth in that nematode. In previous studies FEZ1 has been found to interact with protein kinase C{zeta}, DISC1, the agnoprotein of the human polyomavirus JC virus, and E4B, a U-box-type ubiquitin-protein isopeptide ligase. We reported previously that FEZ1 and its paralogue FEZ2 are proteins that interact with NEK1, a protein kinase involved in polycystic kidney disease and DNA repair mechanisms at the G2/M phase of the cell cycle. Here we report the identification of 16 proteins that interact with human FEZ1-(221-396) in a yeast two-hybrid assay of a human fetal brain cDNA library. The 13 interacting proteins of known functions take part either in transcription regulation and chromatin remodeling (6 proteins), the regulation of neuronal cell development (2 proteins) and cellular transport mechanisms (3 proteins) or participate in apoptosis (2 proteins). We were able to confirm eight of the observed interactions by in vitro pull-down assays with recombinant fusion proteins. The confirmed interacting proteins include FEZ1 itself and three transcription controlling proteins (SAP30L, DRAP1, and BAF60a). In mapping studies we found that the C-terminal regions of FEZ1, and especially its coiled-coil region, are involved in its dimerization, its heterodimerization with FEZ2, and in the interaction with 10 of the identified interacting proteins. Our results give further support to the previous speculation of the functional involvement of FEZ1 in neuronal development but suggest further that FEZ1 may also be involved in transcriptional control. 10.1074/jbc.M513280200}, author = {Assmann, Eliana M. and Alborghetti, Marcos R. and Camargo, Maria E. and Kobarg, Jorg}, citeulike-article-id = {1560346}, citeulike-linkout-0 = {http://dx.doi.org/10.1074/jbc.M513280200}, citeulike-linkout-1 = {http://www.jbc.org/cgi/content/abstract/281/15/9869}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/16484223}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=16484223}, day = {14}, doi = {10.1074/jbc.M513280200}, journal = {J. Biol. Chem.}, keywords = {axon, axon-guidance, axonal-transport, dendrin, dendritic-compartment, dendritic-mrna, fez1}, month = {April}, number = {15}, pages = {9869--9881}, posted-at = {2007-08-14 14:54:26}, priority = {2}, title = {FEZ1 Dimerization and Interaction with Transcription Regulatory Proteins Involves Its Coiled-coil Region}, url = {http://dx.doi.org/10.1074/jbc.M513280200}, volume = {281}, year = {2006} }

TY - JOUR ID - citeulike:1560346 L3 - citeulike-article-id:1560346 N2 - The fasciculation and elongation protein {zeta}1 (FEZ1) is a mammalian orthologue of the Caenorhabditis elegans protein UNC-76, which is necessary for axon growth in that nematode. In previous studies FEZ1 has been found to interact with protein kinase C{zeta}, DISC1, the agnoprotein of the human polyomavirus JC virus, and E4B, a U-box-type ubiquitin-protein isopeptide ligase. We reported previously that FEZ1 and its paralogue FEZ2 are proteins that interact with NEK1, a protein kinase involved in polycystic kidney disease and DNA repair mechanisms at the G2/M phase of the cell cycle. Here we report the identification of 16 proteins that interact with human FEZ1-(221-396) in a yeast two-hybrid assay of a human fetal brain cDNA library. The 13 interacting proteins of known functions take part either in transcription regulation and chromatin remodeling (6 proteins), the regulation of neuronal cell development (2 proteins) and cellular transport mechanisms (3 proteins) or participate in apoptosis (2 proteins). We were able to confirm eight of the observed interactions by in vitro pull-down assays with recombinant fusion proteins. The confirmed interacting proteins include FEZ1 itself and three transcription controlling proteins (SAP30L, DRAP1, and BAF60a). In mapping studies we found that the C-terminal regions of FEZ1, and especially its coiled-coil region, are involved in its dimerization, its heterodimerization with FEZ2, and in the interaction with 10 of the identified interacting proteins. Our results give further support to the previous speculation of the functional involvement of FEZ1 in neuronal development but suggest further that FEZ1 may also be involved in transcriptional control. 10.1074/jbc.M513280200 IS - 15 JF - J. Biol. Chem. EP - 9881 TI - FEZ1 Dimerization and Interaction with Transcription Regulatory Proteins Involves Its Coiled-coil Region VL - 281 SP - 9869 KW - axon KW - axon-guidance KW - axonal-transport KW - dendrin KW - dendritic-compartment KW - dendritic-mrna KW - fez1 AU - Assmann, Eliana AU - Alborghetti, Marcos AU - Camargo, Maria AU - Kobarg, Jorg PY - 2006/04/14/ UR - http://dx.doi.org/10.1074/jbc.M513280200 ER -