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primary topic: Structural Analysis of gamma-Tubulin Complexes by Cryo-EM

Structural Analysis of gamma-Tubulin Complexes by Cryo-EM
type: Article
abstract: The cytoskeleton is an essential component of cells composed of three types of polymer networks- actin filaments, intermediate filaments and microtubules. Together they ensure compartmentation, spatial and temporal regulation of cargo flow and regulate the cell shape. Microtubules, the largest polymers of the cytoskeleton, are hollow cylinders composed of alpha/beta-tubulin dimers arranged in protofilaments. The orientation of alpha/beta-tubulin dimers in protofilaments is giving rise to the polarity of microtubules with the beta-tubulin-facing plus end and the alpha/-tubulin-facing minus end. The microtubule plus end is dynamic while the minus end is the origin of microtubule nucleation. In cells, microtubules are formed de novo in a process termed microtubule nucleation that is mediated by gamma-TuCs composed of gamma-tubulins and gamma-complex proteins (GCPs). These complexes serve as structural templates for microtubule nucleation, accelerating the process by decreasing an initial kinetic barrier. In fungi, the principal microtubule template is the gamma-TuSC, which is assembled from Spc97 and Spc98 and two copies of gamma-tubulin, and oligomerizes at the SPB into a ring-like structure templating microtubule nucleation. The vertebrate principal microtubule template, the gamma-TuRC, is compositionally more complex. Besides containing homologs of fungal Spc97 and Spc98 termed GCP2 and GCP3, respectively, three additional GCP variants-GCP4, GCP5 and GCP6 - are present as well. Structural studies of the gamma-TuRC have been not successful, preventing description of its molecular architecture and geometry and cryo-EM of the gamma-TuSC reached only a medium resolution not allowing to elucidate details as an interface on a residue level or small conformational differences. In this study, I present detailed structures of both types of gamma-TuCs complemented with biological approaches performed by my collaborators. Using cryo-EM and negative stain EM analysis, I gained …
date: 2022
author list: authors
type: EPrint
type: DoctoralThesisEPrint
is part of: repository
has document: Structural Analysis of gamma-Tubulin Complexes by Cryo-EM (PDF)
has document: Structural Analysis of gamma-Tubulin Complexes by Cryo-EM (Other)
subject: 570 Biowissenschaften, Biologie

Structural Analysis of gamma-Tubulin Complexes by Cryo-EM (PDF)
type: Document
has file: Phd_thesis_final_electronic_version_PDFA.pdf
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Erik Zupa
type: Person
given name: Erik
family name: Zupa

Structural Analysis of gamma-Tubulin Complexes by Cryo-EM (Other)
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Structural Analysis of gamma-Tubulin Complexes by Cryo-EM (Other)
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primary topic: Structural Analysis of gamma-Tubulin Complexes by Cryo-EM

570 Biowissenschaften, Biologie
type: Concept
preferred label: 570 Life sciences @en