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Vol. 8, Issue 11, 2187-2198, November 1997
Department of Physiology, Boston University School of Medicine,
Boston, Massachusetts 02118
When ciliogenesis first occurs in sea urchin embryos, the major
building block proteins, tubulin and dynein, exist in substantial pools, but most 9+2 architectural proteins must be synthesized de novo.
Pulse-chase labeling with [3H]leucine demonstrates that
these proteins are coordinately up-regulated in response to deciliation
so that regeneration ensues and the tubulin and dynein pools are
replenished. Protein labeling and incorporation into already-assembled
cilia is high, indicating constitutive ciliary gene expression and
steady-state turnover. To determine whether either the synthesis of
tubulin or the size of its available pool is coupled to the synthesis
or turnover of the other 9+2 proteins in some feedback manner,
fully-ciliated mid- or late-gastrula stage Strongylocentrotus
droebachiensis embryos were pulse labeled in the presence of
colchicine or taxol at concentrations that block ciliary growth. As a
consequence of tubulin autoregulation mediated by increased free
tubulin, no labeling of ciliary tubulin occurred in colchicine-treated embryos. However, most other proteins were labeled and incorporated into steady-state cilia at near-control levels in the presence of
colchicine or taxol. With taxol, tubulin was labeled as well. An
axoneme-associated 78 kDa cognate of the molecular chaperone HSP70
correlated with length during regeneration; neither colchicine nor
taxol influenced the association of this protein in steady-state cilia.
These data indicate that 1) ciliary protein synthesis and turnover is
independent of tubulin synthesis or tubulin pool size; 2) steady-state
incorporation of labeled proteins cannot be due to formation or
elongation of cilia; 3) substantial tubulin exchange takes place in
fully-motile cilia; and 4) chaperone presence and association in
steady-state cilia is independent of background ciliogenesis, tubulin
synthesis, and tubulin assembly state.
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