PMID- 10085260
OWN - NLM
STAT- MEDLINE
DCOM- 19990719
LR  - 20151119
IS  - 0021-9533 (Print)
IS  - 0021-9533 (Linking)
VI  - 112 ( Pt 8)
DP  - 1999 Apr
TI  - The growth-related, translationally controlled protein P23 has properties of a
      tubulin binding protein and associates transiently with microtubules during the
      cell cycle.
PG  - 1257-71
AB  - The translationally controlled protein P23 was discovered by the early induction 
      of its rate of synthesis after mitogenic stimulation of mouse fibroblasts. P23 is
      expressed in almost all mammalian tissues and it is highly conserved between
      animals, plants and yeast. Based on its amino acid sequence, P23 cannot be
      attributed to any known protein family, and its cellular function remains to be
      elucidated. Here, we present evidence that P23 has properties of a tubulin
      binding protein that associates with microtubules in a cell cycle-dependent
      manner. (1) P23 is a cytoplasmic protein that occurs in complexes of 100-150 kDa,
      and part of P23 can be immunoprecipitated from HeLa cell extracts with
      anti-tubulin antibodies. (2) In immunolocalisation experiments we find P23
      associated with microtubules during G1, S, G2 and early M phase of the cell
      cycle. At metaphase, P23 is also bound to the mitotic spindle, and it is detached
      from the spindle during metaphase-anaphase transition. (3) A GST-P23 fusion
      protein interacts with alpha- and beta-tubulin, and recombinant P23 binds to
      taxol-stabilised microtubules in vitro. The tubulin binding domain of P23 was
      identified by mutational analysis; it shows similarity to part of the tubulin
      binding domain of the microtubule-associated protein MAP-1B. (4) Overexpression
      of P23 results in cell growth retardation and in alterations of cell morphology. 
      Moreover, elevation of P23 levels leads to microtubule rearrangements and to an
      increase in microtubule mass and stability.
FAU - Gachet, Y
AU  - Gachet Y
AD  - Divisions of Biochemistry and Immunology, St George's Hospital Medical School,
      London, UK.
FAU - Tournier, S
AU  - Tournier S
FAU - Lee, M
AU  - Lee M
FAU - Lazaris-Karatzas, A
AU  - Lazaris-Karatzas A
FAU - Poulton, T
AU  - Poulton T
FAU - Bommer, U A
AU  - Bommer UA
LA  - eng
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Cell Sci
JT  - Journal of cell science
JID - 0052457
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Tubulin)
RN  - 0 (tumor protein, translationally-controlled 1)
RN  - SH1WY3R615 (Nocodazole)
SB  - IM
MH  - 3T3 Cells
MH  - Acetylation
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Biomarkers, Tumor
MH  - Blotting, Western
MH  - COS Cells
MH  - Calcium-Binding Proteins/*physiology
MH  - Carrier Proteins/*physiology
MH  - Cattle
MH  - *Cell Cycle
MH  - Cell Division
MH  - Cytoplasm/metabolism
MH  - Cytoskeleton/metabolism
MH  - Epithelial Cells
MH  - Escherichia coli/metabolism
MH  - Flow Cytometry
MH  - Fluorescent Antibody Technique
MH  - HeLa Cells
MH  - Humans
MH  - Mice
MH  - Microtubules/*metabolism
MH  - Models, Genetic
MH  - Molecular Sequence Data
MH  - Nocodazole/pharmacology
MH  - Recombinant Fusion Proteins
MH  - Sequence Homology, Amino Acid
MH  - Subcellular Fractions
MH  - Time Factors
MH  - Transfection
MH  - Tubulin/*metabolism
EDAT- 1999/03/23 00:00
MHDA- 1999/03/23 00:01
CRDT- 1999/03/23 00:00
PHST- 1999/03/23 00:00 [pubmed]
PHST- 1999/03/23 00:01 [medline]
PHST- 1999/03/23 00:00 [entrez]
PST - ppublish
SO  - J Cell Sci. 1999 Apr;112 ( Pt 8):1257-71.