The centrosomal localization of KM-HN-1 (MGC33607) depends on the leucine zipper motif and the C-terminal coiled-coil domain.
- Author:
Hye Jeong PARK
1
;
Hyun Joo SEO
;
Hyun Woo KIM
;
Jung Soon KIM
;
So Yoon HWANG
;
Yeon Sun SEONG
Author Information
1. Department of Biochemistry, College of Medicine, Dankook University, Cheonan 330-714, Korea. seongys@dku.edu
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
CDC110 protein, human;
cell nucleus;
centrosome;
protein structure, tertiary;
protein transport
- MeSH:
Amino Acid Motifs/physiology;
Amino Acid Sequence;
Antigens, Neoplasm/chemistry/*metabolism;
Cells, Cultured;
Centrosome/*metabolism;
Fluorescent Antibody Technique;
Humans;
Leucine Zippers/*physiology;
Molecular Sequence Data;
Mutation;
Nuclear Proteins/chemistry/*metabolism;
Protein Conformation;
Protein Structure, Tertiary;
Sequence Analysis, Protein
- From:Experimental & Molecular Medicine
2007;39(6):828-838
- CountryRepublic of Korea
- Language:English
-
Abstract:
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.
