Abstract
Tau is abundant in the axon, whereas MAP2 is found in the cell body and dendrites. To understand their differential localization, we performed transfection studies on primary cultured neurons using tagged tau, MAP2, MAP2C, and their chimeric/deletion mutants. We found that MAP2 was prevented from entering the axon by its N-terminal projection domain and that microtubule binding of tau was stronger in the axon than in the cell body and dendrites, whereas that of MAP2/MAP2C was tighter in the cell body and dendrites than in the axon. These binding properties were determined by their microtubule-binding domains and were suggested to be regulated by phosphorylation, at least in the case of tau. Thus, the suppressed axonal transit of MAP2 and locally regulated microtubule binding may play important roles for their sorting in neurons.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Axons / physiology*
-
Axons / ultrastructure
-
Cells, Cultured
-
Dendrites / physiology
-
Dendrites / ultrastructure
-
Embryo, Mammalian
-
Fluorescent Antibody Technique
-
In Situ Hybridization
-
Mice / immunology
-
Microtubule-Associated Proteins / analysis
-
Microtubule-Associated Proteins / biosynthesis
-
Microtubule-Associated Proteins / metabolism*
-
Microtubules / physiology*
-
Microtubules / ultrastructure
-
Molecular Sequence Data
-
Neurons / physiology*
-
Protein Binding
-
Proto-Oncogene Proteins c-myc / analysis
-
Proto-Oncogene Proteins c-myc / biosynthesis
-
Proto-Oncogene Proteins c-myc / metabolism
-
Sequence Homology, Amino Acid
-
Sheep / immunology
-
Spinal Cord / physiology
-
Transfection
-
tau Proteins / analysis
-
tau Proteins / biosynthesis
-
tau Proteins / metabolism*
Substances
-
Microtubule-Associated Proteins
-
Proto-Oncogene Proteins c-myc
-
tau Proteins