At least one of the protofilaments in flagellar microtubules is not composed of tubulin

Nojima, Dana; Linck, Richard W.; Egelman, Edward H.

doi:10.1016/s0960-9822(95)00037-6

Cited by 80 publications

(73 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Consequently, these proteins are potentially accessible for exchange with their soluble or transported counterparts. An apparent exception is tektin-A, an integral structural determinant of certain doublet microtubule protofilaments (Nojima et al, 1995). However, biochemically there are two subclasses of tektin-A, one readily soluble in chaotropic agents and one not.…”

Section: Discussionmentioning

confidence: 99%

Synthesis and Turnover of Embryonic Sea Urchin Ciliary Proteins during Selective Inhibition of Tubulin Synthesis and Assembly

Stephens

1997

MBoC

View full text Add to dashboard Cite

When ciliogenesis first occurs in sea urchin embryos, the major building block proteins, tubulin and dynein, exist in substantial pools, but most 9ϩ2 architectural proteins must be synthesized de novo. Pulse-chase labeling with [3 H]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 9ϩ2 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 colchicinetreated 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.

show abstract

Section: Discussionmentioning

confidence: 99%

Synthesis and Turnover of Embryonic Sea Urchin Ciliary Proteins during Selective Inhibition of Tubulin Synthesis and Assembly

Stephens

1997

MBoC

View full text Add to dashboard Cite

show abstract

“…1, has a number of compelling advantages. Aside from the historic precedent of the base-totip CCW numbering [Tilney et al, 1973;Linck, 1976;Nojima et al, 1995;Song and Mandelkow, 1995;Nicastro et al, 2006;Setter et al, 2006], a CCW convention permits PF B 10 to lie adjacent to the ephemeral B-11th component, rather than the more confusing CW juxtaposition of PF B 1 and the B-11th component. Even though the B-11th component will eventually be identified and appropriately named, there are a sufficient number of reports of its existence that its adjacent B-tubulin PF be numbered B 10 .…”

Section: Proposed Numbering Conventionmentioning

confidence: 99%

Functional protofilament numbering of ciliary, flagellar, and centriolar microtubules

Linck

Stephens

2007

Cell Motil. Cytoskeleton

Self Cite

View full text Add to dashboard Cite

show abstract

“…Treatment with urea removes tubulin and leaves a stable filamentous structure. These tektin filaments are components of the threestranded ribbons and may form one of the protofilaments of the A tubule [Nojima et al, 1995].…”

Section: Introductionmentioning

confidence: 99%

Axonemal protofilament ribbons, DM10 domains, and the link to juvenile myoclonic epilepsy

King

2006

Cell Motil. Cytoskeleton

View full text Add to dashboard Cite

Juvenile myoclonic epilepsy (JME) is a common neurological disorder that results in short uncontrolled muscle contractions and sometimes more severe seizures. Genetic studies have suggested that JME may be caused by mutations in EFHC1. The Efhc1 protein consists of three DM10 domains and a C-terminal region containing a potential Ca 2þ -binding motif. In Chlamydomonas, a protein (Rib72) of almost identical domain structure is a component of the protofilament ribbons within the doublet microtubules of the flagellar axoneme. Here I discuss recent work that supports assignment of human Efhc1 as a ciliary component and the resulting implications for the mechanism of disease causation. Cell Motil.

show abstract

At least one of the protofilaments in flagellar microtubules is not composed of tubulin

Cited by 80 publications

References 37 publications

Synthesis and Turnover of Embryonic Sea Urchin Ciliary Proteins during Selective Inhibition of Tubulin Synthesis and Assembly

Synthesis and Turnover of Embryonic Sea Urchin Ciliary Proteins during Selective Inhibition of Tubulin Synthesis and Assembly

Functional protofilament numbering of ciliary, flagellar, and centriolar microtubules

Axonemal protofilament ribbons, DM10 domains, and the link to juvenile myoclonic epilepsy

Contact Info

Product

Resources

About