Abstract
Factors that regulate the microtubule cytoskeleton are critical in determining cell behavior. Here we describe the function of a novel protein that we term E-like based on its sequence similarity to the tubulin-specific chaperone cofactor E. We find that upon overexpression, E-like depolymerizes microtubules by committing tubulin to proteosomal degradation. Our data suggest that this function is direct and is based on the ability of E-like to disrupt the tubulin heterodimer in vitro. Suppression of E-like expression results in an increase in the number of stable microtubules and a tight clustering of endocellular membranes around the microtubule-organizing center, while the properties of dynamic microtubules are unaffected. These observations define E-like as a novel regulator of tubulin stability, and provide a link between tubulin turnover and vesicle transport.
Publication types
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Blotting, Northern
-
Brain / metabolism
-
Caenorhabditis elegans
-
Cattle
-
Cell Membrane / metabolism
-
Cytoskeleton / metabolism
-
Cytosol / metabolism
-
DNA, Complementary / metabolism
-
Dimerization
-
Escherichia coli / metabolism
-
Expressed Sequence Tags
-
GTP Phosphohydrolases / chemistry
-
Green Fluorescent Proteins / metabolism
-
HeLa Cells
-
Humans
-
Immunoblotting
-
Microscopy, Fluorescence
-
Microtubule-Associated Proteins / chemistry*
-
Microtubule-Associated Proteins / physiology*
-
Microtubules / metabolism
-
Molecular Chaperones / chemistry*
-
Molecular Chaperones / physiology
-
Molecular Sequence Data
-
Phylogeny
-
Plasmids / metabolism
-
Proteasome Endopeptidase Complex / metabolism
-
Protein Binding
-
Protein Folding
-
RNA, Small Interfering / metabolism
-
Sequence Homology, Amino Acid
-
Tissue Distribution
-
Transfection
-
Tubulin / chemistry
Substances
-
DNA, Complementary
-
Microtubule-Associated Proteins
-
Molecular Chaperones
-
RNA, Small Interfering
-
TBCE protein, human
-
TBCEL protein, human
-
Tubulin
-
Green Fluorescent Proteins
-
Proteasome Endopeptidase Complex
-
GTP Phosphohydrolases