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Receptors determine the cellular localization of a gamma-tubulin complex and thereby the site of microtubule formation
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
9670012
retrieved
1 December 2016
title
Receptors determine the cellular localization of a gamma-tubulin complex and thereby the site of microtubule formation
(English)
1 reference
stated in
PubMed
PubMed ID
9670012
retrieved
1 December 2016
main subject
microtubule
0 references
Gamma-tubulin complex subunit SPC72 YAL047C
1 reference
stated in
GOA release 2020-03-11
Spc97p YHR172W
1 reference
stated in
GOA release 2020-03-11
author name string
M Knop
series ordinal
1
0 references
E Schiebel
series ordinal
2
0 references
language of work or name
English
0 references
publication date
15 July 1998
0 references
published in
The EMBO Journal
1 reference
stated in
PubMed
PubMed ID
9670012
retrieved
1 December 2016
volume
17
0 references
page(s)
3952-67
0 references
issue
14
0 references
cites work
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Spc98p and Spc97p of the yeast gamma-tubulin complex mediate binding to the spindle pole body via their interaction with Spc110p
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The spacer protein Spc110p targets calmodulin to the central plaque of the yeast spindle pole body.
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Heterologous HIS3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae
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Nucleation of microtubule assembly by a gamma-tubulin-containing ring complex
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Spc98p directs the yeast gamma-tubulin complex into the nucleus and is subject to cell cycle-dependent phosphorylation on the nuclear side of the spindle pole body
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Spc110p: assembly properties and role in the connection of nuclear microtubules to the yeast spindle pole body
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gamma-Tubulin-like Tub4p of Saccharomyces cerevisiae is associated with the spindle pole body substructures that organize microtubules and is required for mitotic spindle formation
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29 September 2017
The spindle pole body component Spc98p interacts with the gamma-tubulin-like Tub4p of Saccharomyces cerevisiae at the sites of microtubule attachment
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29 September 2017
The 110-kD spindle pole body component of Saccharomyces cerevisiae is a phosphoprotein that is modified in a cell cycle-dependent manner
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29 September 2017
A highly divergent gamma-tubulin gene is essential for cell growth and proper microtubule organization in Saccharomyces cerevisiae
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29 September 2017
Disruption of mitotic spindle orientation in a yeast dynein mutant
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29 September 2017
In vitro reconstitution of centrosome assembly and function: the central role of gamma-tubulin
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29 September 2017
The centrosome and cellular organization
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29 September 2017
gamma-tubulin is a minus end-specific microtubule binding protein
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29 September 2017
Microtubule-nucleating activity of centrosomes in Chinese hamster ovary cells is independent of the centriole cycle but coupled to the mitotic cycle
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29 September 2017
Microtubule organizing centers
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PubMed Central
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29 September 2017
Isolation of mip (microtubule-interacting protein) mutations of Aspergillus nidulans
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29 September 2017
Genetic analysis of the yeast cytoskeleton.
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29 September 2017
In vitro microtubule-nucleating activity of spindle pole bodies in fission yeast Schizosaccharomyces pombe: cell cycle-dependent activation in xenopus cell-free extracts
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PubMed Central
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29 September 2017
Role of astral microtubules and actin in spindle orientation and migration in the budding yeast, Saccharomyces cerevisiae
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PubMed Central
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29 September 2017
Astral microtubules are not required for anaphase B in Saccharomyces cerevisiae
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PubMed Central
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29 September 2017
Spindle poles in higher plant mitosis
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PubMed Central
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29 September 2017
Microbial Determinations by Flow Cytometry
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29 September 2017
The spindle pole body component Spc97p interacts with the gamma-tubulin of Saccharomyces cerevisiae and functions in microtubule organization and spindle pole body duplication
1 reference
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PubMed Central
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2 June 2018
Centrosome-microtubule nucleation.
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2 June 2018
Spc42p: a phosphorylated component of the S. cerevisiae spindle pole body (SPD) with an essential function during SPB duplication
1 reference
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PubMed Central
reference URL
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2 June 2018
A spacer protein in the Saccharomyces cerevisiae spindle poly body whose transcript is cell cycle-regulated
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PubMed Central
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2 June 2018
Preparation of yeast cells for thin-section electron microscopy
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PubMed Central
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2 June 2018
The fission yeast gamma-tubulin is essential for mitosis and is localized at microtubule organizing centers.
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PubMed Central
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2 June 2018
Gamma-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation
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PubMed Central
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2 June 2018
Identification of gamma-tubulin, a new member of the tubulin superfamily encoded by mipA gene of Aspergillus nidulans.
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20 June 2018
Isolated Plant Nuclei Nucleate Microtubule Assembly: The Nuclear Surface in Higher Plants Has Centrosome-like Activity
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PubMed
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12 December 2020
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Characterization of gamma-tubulin complexes in Aspergillus nidulans and detection of putative gamma-tubulin interacting proteins
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/9670012
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12 December 2020
based on heuristic
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The use of cell division cycle mutants to investigate the control of microtubule distribution in the fission yeast Schizosaccharomyces pombe
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PubMed
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12 December 2020
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Microtubule assembly nucleated by isolated centrosomes
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PubMed
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
A gamma-tubulin-related protein associated with the microtubule arrays of higher plants in a cell cycle-dependent manner
1 reference
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PubMed
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https://pubmed.ncbi.nlm.nih.gov/9670012
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Gamma-tubulin is a component of the spindle pole body that is essential for microtubule function in Aspergillus nidulans
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9670012
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
The Phosphorylation State of the 110 kDa Component of the Yeast Spindle Pole Body Shows Cell Cycle Dependent Regulation
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9670012
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1093/EMBOJ/17.14.3952
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1781916
OpenCitations bibliographic resource ID
1781916
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1781916
PMCID
1170730
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1781916
PubMed ID
9670012
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1781916
ResearchGate publication ID
13614984
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