Structure of the microtubule anchoring factor NEDD1 bound to the γ-tubulin ring complex DOI Creative Commons
Hugo Muñoz-Hernández, Yixin Xu, Daniel Y. Zhang

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Nov. 5, 2024

The γ-tubulin ring complex (γ-TuRC) is an essential multiprotein assembly, in which γ-tubulin, GCP2-6, actin, MZT1 and MZT2 form asymmetric cone-shaped structure that provides a template for microtubule nucleation. γ-TuRC recruited to organizing centers (MTOCs), such as centrosomes pre-existing mitotic spindle microtubules, via the evolutionarily-conserved attachment factor NEDD1. NEDD1 contains N-terminal WD40 domain binds C-terminal associates with γ-TuRC. However, structural basis of NEDD1-γ-TuRC interaction not known. Here, we report cryo-electron microscopy (cryo-EM) structures bound human absence or presence activating CDK5RAP2, interacts GCP2 induce conformational changes promote its nucleating function. We found C-terminus forms tetrameric α-helical assembly contacts lumen cone, anchored GCP4, 5 6 protein modules consisting & GCP3 subcomplexes, orients microtubule-binding domains away from complex. biochemically tested our models by identifying mutants unable pull-down

Language: Английский

MZT1 protects gastric cancer against glucose starvation through targeting NEDD1 DOI
Ruiyang Zhao, Bo Cao,

Hanghang Li

et al.

Life Sciences, Journal Year: 2025, Volume and Issue: unknown, P. 123622 - 123622

Published: April 1, 2025

Language: Английский

Citations

0
Structure of the microtubule-anchoring factor NEDD1 bound to the γ-tubulin ring complex DOI Creative Commons
Hugo Muñoz-Hernández, Yixin Xu,

Aitor Pellicer Camardiel

et al.

The Journal of Cell Biology, Journal Year: 2025, Volume and Issue: 224(8)

Published: May 21, 2025

The γ-tubulin ring complex (γ-TuRC) is an essential multiprotein assembly that provides a template for microtubule nucleation. γ-TuRC recruited to microtubule-organizing centers (MTOCs) by the evolutionarily conserved attachment factor NEDD1. However, structural basis of NEDD1–γ-TuRC interaction not known. Here, we report cryo-EM structures NEDD1 bound human in absence or presence activating CDK5RAP2. We found C-terminus forms tetrameric α-helical contacts lumen cone and orients its microtubule-binding domain away from complex. structure simultaneously CDK5RAP2 reveals both factors can associate with “open” conformation Our results show does induce substantial conformational changes but suggest anchoring γ-TuRC–capped microtubules would be structurally compatible significant experienced during

Language: Английский

Citations

0
Structure of the microtubule anchoring factor NEDD1 bound to the γ-tubulin ring complex DOI Creative Commons
Hugo Muñoz-Hernández, Yixin Xu, Daniel Y. Zhang

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Nov. 5, 2024

The γ-tubulin ring complex (γ-TuRC) is an essential multiprotein assembly, in which γ-tubulin, GCP2-6, actin, MZT1 and MZT2 form asymmetric cone-shaped structure that provides a template for microtubule nucleation. γ-TuRC recruited to organizing centers (MTOCs), such as centrosomes pre-existing mitotic spindle microtubules, via the evolutionarily-conserved attachment factor NEDD1. NEDD1 contains N-terminal WD40 domain binds C-terminal associates with γ-TuRC. However, structural basis of NEDD1-γ-TuRC interaction not known. Here, we report cryo-electron microscopy (cryo-EM) structures bound human absence or presence activating CDK5RAP2, interacts GCP2 induce conformational changes promote its nucleating function. We found C-terminus forms tetrameric α-helical assembly contacts lumen cone, anchored GCP4, 5 6 protein modules consisting & GCP3 subcomplexes, orients microtubule-binding domains away from complex. biochemically tested our models by identifying mutants unable pull-down

Language: Английский

Citations

1