Exp Mol Med.  2007 Dec;39(6):828-838.

The centrosomal localization of KM-HN-1 (MGC33607) depends on the leucine zipper motif and the C-terminal coiled-coil domain

Affiliations
  • 1Department of Biochemistry, College of Medicine, Dankook University, Cheonan 330-714, Korea. seongys@dku.edu

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.

Keyword

CDC110 protein, human; cell nucleus; centrosome; protein structure, tertiary; protein transport

MeSH Terms

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
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