Insight into microtubule nucleation from tubulin-capping proteins. 2019

Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France.

Nucleation is one of the least understood steps of microtubule dynamics. It is a kinetically unfavorable process that is templated in the cell by the γ-tubulin ring complex or by preexisting microtubules; it also occurs in vitro from pure tubulin. Here we study the nucleation inhibition potency of natural or artificial proteins in connection with their binding mode to the longitudinal surface of α- or β-tubulin. The structure of tubulin-bound CopN, a Chlamydia protein that delays nucleation, suggests that this protein may interfere with two protofilaments at the (+) end of a nucleus. Designed ankyrin repeat proteins that share a binding mode similar to that of CopN also impede nucleation, whereas those that target only one protofilament do not. In addition, an αRep protein predicted to target two protofilaments at the (-) end does not delay nucleation, pointing to different behaviors at both ends of the nucleus. Our results link the interference with protofilaments at the (+) end and the inhibition of nucleation.

UI MeSH Term Description Entries
D008870 Microtubules Slender, cylindrical filaments found in the cytoskeleton of plant and animal cells. They are composed of the protein TUBULIN and are influenced by TUBULIN MODULATORS. Microtubule
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D014404 Tubulin A microtubule subunit protein found in large quantities in mammalian brain. It has also been isolated from SPERM FLAGELLUM; CILIA; and other sources. Structurally, the protein is a dimer with a molecular weight of approximately 120,000 and a sedimentation coefficient of 5.8S. It binds to COLCHICINE; VINCRISTINE; and VINBLASTINE. alpha-Tubulin,beta-Tubulin,delta-Tubulin,epsilon-Tubulin,gamma-Tubulin,alpha Tubulin,beta Tubulin,delta Tubulin,epsilon Tubulin,gamma Tubulin
D016993 Chlamydophila pneumoniae A species of CHLAMYDOPHILA that causes acute respiratory infection, especially atypical pneumonia, in humans, horses, and koalas. Chlamydia pneumoniae

Related Publications

Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
July 2011, Nature structural & molecular biology,
Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
December 2002, The Journal of biological chemistry,
Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
May 2005, Nature,
Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
November 1977, Journal of molecular biology,
Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
October 2006, Journal of cell science,
Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
October 2011, Nature reviews. Molecular cell biology,
Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
April 2001, Current opinion in structural biology,
Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
February 2021, Current opinion in cell biology,
Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
January 2022, Frontiers in cell and developmental biology,
Valérie Campanacci, and Agathe Urvoas, and Soraya Cantos-Fernandes, and Magali Aumont-Nicaise, and Ana-Andreea Arteni, and Christophe Velours, and Marie Valerio-Lepiniec, and Birgit Dreier, and Andreas Plückthun, and Antoine Pilon, and Christian Poüs, and Philippe Minard, and Benoît Gigant
September 2017, Cell reports,
Copied contents to your clipboard!