Cargando…

Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation

Budding yeast Spc110, a member of γ-tubulin complex receptor family (γ-TuCR), recruits γ-tubulin complexes to microtubule (MT) organizing centers (MTOCs). Biochemical studies suggest that Spc110 facilitates higher-order γ-tubulin complex assembly (Kollman et al., 2010). Nevertheless the molecular ba...

Descripción completa

Detalles Bibliográficos
Autores principales:	Lin, Tien-chen, Neuner, Annett, Schlosser, Yvonne T, Scharf, Annette ND, Weber, Lisa, Schiebel, Elmar
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	eLife Sciences Publications, Ltd 2014
Materias:	Biochemistry
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4034690/ https://www.ncbi.nlm.nih.gov/pubmed/24842996 http://dx.doi.org/10.7554/eLife.02208

Ejemplares similares

The microtubule polymerase Stu2 promotes oligomerization of the γ-TuSC for cytoplasmic microtubule nucleation
por: Gunzelmann, Judith, et al.
Publicado: (2018)

The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems
por: Zupa, Erik, et al.
Publicado: (2020)

MOZART1 and γ-tubulin complex receptors are both required to turn γ-TuSC into an active microtubule nucleation template
por: Lin, Tien-chen, et al.
Publicado: (2016)

Microtubule nucleating γTuSC assembles structures with 13-fold microtubule-like symmetry
por: Kollman, Justin M., et al.
Publicado: (2010)

Modular assembly of the principal microtubule nucleator γ-TuRC
por: Würtz, Martin, et al.
Publicado: (2022)

An extended γ-tubulin ring functions as a stable platform in microtubule nucleation
por: Erlemann, Sarah, et al.
Publicado: (2012)

Interaction of CK1δ with γTuSC ensures proper microtubule assembly and spindle positioning
por: Peng, Yutian, et al.
Publicado: (2015)

Phosphorylation of the Yeast γ-Tubulin Tub4 Regulates Microtubule Function
por: Lin, Tien-chen, et al.
Publicado: (2011)

Microtubule nucleation from the fibrous corona by LIC1-pericentrin promotes chromosome congression
por: Wu, Jingchao, et al.
Publicado: (2023)

The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)
por: Rale, Michael J, et al.
Publicado: (2022)

The Centrosomal Linker and Microtubules Provide Dual Levels of Spatial Coordination of Centrosomes
por: Panic, Marko, et al.
Publicado: (2015)

Biochemical reconstitution of branching microtubule nucleation
por: Alfaro-Aco, Raymundo, et al.
Publicado: (2020)

Genome-wide haploinsufficiency screen reveals a novel role for γ-TuSC in spindle organization and genome stability
por: Choy, John S., et al.
Publicado: (2013)

Nonrandom γ-TuNA-dependent spatial pattern of microtubule nucleation at the Golgi
por: Sanders, Anna A. W. M., et al.
Publicado: (2017)

Pericentrin in health and disease: Exploring the patchwork of Pericentrin splice variants
por: Mühlhans, Johanna, et al.
Publicado: (2012)

Ring closure activates yeast γTuRC for species-specific microtubule nucleation
por: Kollman, Justin M., et al.
Publicado: (2015)

PLK1 phosphorylation of pericentrin initiates centrosome maturation at the onset of mitosis
por: Lee, Kwanwoo, et al.
Publicado: (2011)

Drosophila melanogaster γ-TuRC is dispensable for targeting γ-tubulin to the centrosome and microtubule nucleation
por: Vérollet, Christel, et al.
Publicado: (2006)

Microtubule Nucleation Properties of Single Human γTuRCs Explained by Their Cryo-EM Structure
por: Consolati, Tanja, et al.
Publicado: (2020)

Microtubule nucleation and γTuRC centrosome localization in interphase cells require ch-TOG
por: Ali, Aamir, et al.
Publicado: (2023)

The augmin complex architecture reveals structural insights into microtubule branching
por: Zupa, Erik, et al.
Publicado: (2022)

Methylene blue inhibits nucleation and elongation of SOD1 amyloid fibrils
por: Musteikyte, Greta, et al.
Publicado: (2020)

The N-terminus of Sfi1 and yeast centrin Cdc31 provide the assembly site for a new spindle pole body
por: Rüthnick, Diana, et al.
Publicado: (2021)

A perinuclear α-helix with amphipathic features in Brl1 promotes NPC assembly
por: Vitale, Jlenia, et al.
Publicado: (2022)

Pericentrin pivotal in primary cilia
por: Tuma, Rabiya
Publicado: (2004)

Pericentrin in cellular function and disease
por: Delaval, Benedicte, et al.
Publicado: (2010)

The γ-tubulin-specific inhibitor gatastatin reveals temporal requirements of microtubule nucleation during the cell cycle
por: Chinen, Takumi, et al.
Publicado: (2015)

The transition state and regulation of γ-TuRC-mediated microtubule nucleation revealed by single molecule microscopy
por: Thawani, Akanksha, et al.
Publicado: (2020)

Autoinhibition of Cnn binding to γ-TuRCs prevents ectopic microtubule nucleation and cell division defects
por: Tovey, Corinne A., et al.
Publicado: (2021)

Kinesin-14 and kinesin-5 antagonistically regulate microtubule nucleation by γ-TuRC in yeast and human cells
por: Olmsted, Zachary T., et al.
Publicado: (2014)

Chorein sensitive microtubule organization in tumor cells
por: Alkahtani, Saad, et al.
Publicado: (2023)

CEP44 ensures the formation of bona fide centriole wall, a requirement for the centriole-to-centrosome conversion
por: Atorino, Enrico S., et al.
Publicado: (2020)

A Cdk1 phosphomimic mutant of MCAK impairs microtubule end recognition
por: Belsham, Hannah R., et al.
Publicado: (2017)

Duplication and Nuclear Envelope Insertion of the Yeast Microtubule Organizing Centre, the Spindle Pole Body
por: Rüthnick, Diana, et al.
Publicado: (2018)

Polo-like kinase Cdc5 regulates Spc72 recruitment to spindle pole body in the methylotrophic yeast Ogataea polymorpha
por: Maekawa, Hiromi, et al.
Publicado: (2017)

The central scaffold protein CEP350 coordinates centriole length, stability, and maturation
por: Karasu, Onur Rojhat, et al.
Publicado: (2022)

Pathogenic PS1 phosphorylation at Ser367
por: Maesako, Masato, et al.
Publicado: (2017)

Pericentrin interacts with Kinesin-1 to drive centriole motility
por: Hannaford, Matthew R., et al.
Publicado: (2022)

The E3 ligase Poe promotes Pericentrin degradation
por: Galletta, Brian J., et al.
Publicado: (2023)

Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamics
por: Nithianantham, Stanley, et al.
Publicado: (2015)

Cannot write session to /tmp/vufind_sessions/sess_ccgskgfgvn7k5ntjpnd5j5rsas