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Human 76p: A New Member of the γ-Tubulin–Associated Protein Family

The role of the centrosomes in microtubule nucleation remains largely unknown at the molecular level. γ-Tubulin and the two associated proteins h103p (hGCP2) and h104p (hGCP3) are essential. These proteins are also present in soluble complexes containing additional polypeptides. Partial sequencing o...

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Autores principales: Fava, Fabienne, Raynaud-Messina, Brigitte, Leung-Tack, Jeanne, Mazzolini, Laurent, Li, Min, Guillemot, Jean Claude, Cachot, Didier, Tollon, Yvette, Ferrara, Pascual, Wright, Michel
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1999
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2156165/
https://www.ncbi.nlm.nih.gov/pubmed/10562286
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author Fava, Fabienne
Raynaud-Messina, Brigitte
Leung-Tack, Jeanne
Mazzolini, Laurent
Li, Min
Guillemot, Jean Claude
Cachot, Didier
Tollon, Yvette
Ferrara, Pascual
Wright, Michel
author_facet Fava, Fabienne
Raynaud-Messina, Brigitte
Leung-Tack, Jeanne
Mazzolini, Laurent
Li, Min
Guillemot, Jean Claude
Cachot, Didier
Tollon, Yvette
Ferrara, Pascual
Wright, Michel
author_sort Fava, Fabienne
collection PubMed
description The role of the centrosomes in microtubule nucleation remains largely unknown at the molecular level. γ-Tubulin and the two associated proteins h103p (hGCP2) and h104p (hGCP3) are essential. These proteins are also present in soluble complexes containing additional polypeptides. Partial sequencing of a 76- kD polypeptide band from these complexes allowed the isolation of a cDNA encoding for a new protein (h76p = hGCP4) expressed ubiquitously in mammalian tissues. Orthologues of h76p have been characterized in Drosophila and in the higher plant Medicago. Several pieces of evidence indicate that h76p is involved in microtubule nucleation. (1) h76p is localized at the centrosome as demonstrated by immunofluorescence. (2) h76p and γ-tubulin are associated in the γ-tubulin complexes. (3) γ-tubulin complexes containing h76p bind to microtubules. (4) h76p is recruited to the spindle poles and to Xenopus sperm basal bodies. (5) h76p is necessary for aster nucleation by sperm basal bodies and recombinant h76p partially replaces endogenous 76p in oocyte extracts. Surprisingly, h76p shares partial sequence identity with human centrosomal proteins h103p and h104p, suggesting a common protein core. Hence, human γ-tubulin appears associated with at least three evolutionary related centrosomal proteins, raising new questions about their functions at the molecular level.
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spelling pubmed-21561652008-05-01 Human 76p: A New Member of the γ-Tubulin–Associated Protein Family Fava, Fabienne Raynaud-Messina, Brigitte Leung-Tack, Jeanne Mazzolini, Laurent Li, Min Guillemot, Jean Claude Cachot, Didier Tollon, Yvette Ferrara, Pascual Wright, Michel J Cell Biol Original Article The role of the centrosomes in microtubule nucleation remains largely unknown at the molecular level. γ-Tubulin and the two associated proteins h103p (hGCP2) and h104p (hGCP3) are essential. These proteins are also present in soluble complexes containing additional polypeptides. Partial sequencing of a 76- kD polypeptide band from these complexes allowed the isolation of a cDNA encoding for a new protein (h76p = hGCP4) expressed ubiquitously in mammalian tissues. Orthologues of h76p have been characterized in Drosophila and in the higher plant Medicago. Several pieces of evidence indicate that h76p is involved in microtubule nucleation. (1) h76p is localized at the centrosome as demonstrated by immunofluorescence. (2) h76p and γ-tubulin are associated in the γ-tubulin complexes. (3) γ-tubulin complexes containing h76p bind to microtubules. (4) h76p is recruited to the spindle poles and to Xenopus sperm basal bodies. (5) h76p is necessary for aster nucleation by sperm basal bodies and recombinant h76p partially replaces endogenous 76p in oocyte extracts. Surprisingly, h76p shares partial sequence identity with human centrosomal proteins h103p and h104p, suggesting a common protein core. Hence, human γ-tubulin appears associated with at least three evolutionary related centrosomal proteins, raising new questions about their functions at the molecular level. The Rockefeller University Press 1999-11-15 /pmc/articles/PMC2156165/ /pubmed/10562286 Text en © 1999 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Original Article
Fava, Fabienne
Raynaud-Messina, Brigitte
Leung-Tack, Jeanne
Mazzolini, Laurent
Li, Min
Guillemot, Jean Claude
Cachot, Didier
Tollon, Yvette
Ferrara, Pascual
Wright, Michel
Human 76p: A New Member of the γ-Tubulin–Associated Protein Family
title Human 76p: A New Member of the γ-Tubulin–Associated Protein Family
title_full Human 76p: A New Member of the γ-Tubulin–Associated Protein Family
title_fullStr Human 76p: A New Member of the γ-Tubulin–Associated Protein Family
title_full_unstemmed Human 76p: A New Member of the γ-Tubulin–Associated Protein Family
title_short Human 76p: A New Member of the γ-Tubulin–Associated Protein Family
title_sort human 76p: a new member of the γ-tubulin–associated protein family
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2156165/
https://www.ncbi.nlm.nih.gov/pubmed/10562286
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