The centrosomal localization of KM-HN-1 (MGC33607) depends on the leucine zipper motif and the C-terminal coiled-coil domain
Experimental & Molecular Medicine
; : 828-838, 2007.
Article
ي En
| WPRIM
| ID: wpr-62080
المكتبة المسؤولة:
WPRO
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.
Key words
النص الكامل:
1
الفهرس:
WPRIM
الموضوع الرئيسي:
Protein Conformation
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Molecular Sequence Data
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Nuclear Proteins
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Cells, Cultured
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Leucine Zippers
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Fluorescent Antibody Technique
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Amino Acid Sequence
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Protein Structure, Tertiary
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Centrosome
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Sequence Analysis, Protein
المحددات:
Humans
اللغة:
En
مجلة:
Experimental & Molecular Medicine
السنة:
2007
نوع:
Article