Abstract
We isolated Nd1, a novel kelch family gene that encodes two forms of proteins, Nd1-L and Nd1-S. Nd1-L contains a BTB/POZ domain in its N terminus and six kelch repeats in the C terminus. Nd1-S has the BTB/POZ domain but lacks the six kelch repeats. Nd1-L but not Nd1-S mRNA is detected ubiquitously in normal mouse tissues. Nd1-L and Nd1-S proteins can form a dimer through the BTB/POZ domain. Nd1-L colocalizes with actin filaments detected using a confocal microscope, and its kelch repeats bind to them in vitro. Overexpression of Nd1-L in NIH3T3 cells delayed cell growth by affecting the transition of cytokinesis. Furthermore, the overexpression prevented NIH3T3 cells from cell death induced by actin destabilization but not by microtubule dysfunction. These data suggest that Nd1-L functions as a stabilizer of actin filaments as an actin-binding protein and may play a role in the dynamic organization of the actin cytoskeleton.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
3T3 Cells
-
Actins / chemistry*
-
Actins / metabolism
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Animals
-
Base Sequence
-
Blotting, Northern
-
Cell Division
-
Cell Line
-
Cloning, Molecular
-
Cytochalasin D / pharmacology
-
DNA, Complementary / metabolism
-
Epitopes
-
Glutathione Transferase / metabolism
-
Humans
-
Immunoblotting
-
Immunohistochemistry
-
Intracellular Signaling Peptides and Proteins
-
Mice
-
Microscopy, Confocal
-
Microtubules / metabolism
-
Molecular Sequence Data
-
Nucleic Acid Synthesis Inhibitors / pharmacology
-
Precipitin Tests
-
Protein Binding
-
Protein Structure, Tertiary
-
Proteins / chemistry*
-
Proteins / metabolism
-
Proteins / physiology*
-
Recombinant Fusion Proteins / metabolism
-
Sequence Homology, Amino Acid
-
Time Factors
-
Transfection
Substances
-
Actins
-
DNA, Complementary
-
Epitopes
-
Intracellular Signaling Peptides and Proteins
-
Nd1 protein, mouse
-
Nucleic Acid Synthesis Inhibitors
-
Proteins
-
Recombinant Fusion Proteins
-
Cytochalasin D
-
Glutathione Transferase