KMID : 0620920070390060828
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Experimental & Molecular Medicine 2007 Volume.39 No. 6 p.828 ~ p.838
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The centrosomal localization of KM-HN-1 (MGC33607) depends on the leucine zipper motif and the C-terminal coiled-coil domain
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Park Hye-Jeong
Seo Hyun-Joo Kim Hyun-Woo Kim Jung-Soon Hwang So-Yoon Seong Yeon-Sun
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Abstract
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KM-HN-1 is a C-terminal coiled-coil domain containing protein previously referred to as image clone MGC33607. This protein has been previously identified as a cancer/testis antigen and reported as nuclear and chromatin localizing protein. We raised polyclonal antisera with the GST fusion protein and identified them as a 105 kDa protein. Motif analysis showed that this protein harbors the leucine zipper motif in internal 1/3 region and the coiled-coil domain in the C-terminal region. Using the full length and various deletion mutants, we determined the motif that governs the subcellular localization of KM-HN-1. Immunofluorescence staining of the endogenous KM-HN-1 and various kinds of GFP-tagged KM-HN-1 revealed that KM-HN-1 localizes to the centrosomes as well as nucleus. The centrosomal localization-determining region of this protein is C-terminal coiled-coil domain in which the leucine zipper motif and the nuclear export signal (NES) harbor
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KEYWORD
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CCDC110 protein, human, cell nucleus, centrosome, protein structure, tertiary, protein transport
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