Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-12-17
pubmed:databankReference
pubmed:abstractText
The role of the centrosomes in microtubule nucleation remains largely unknown at the molecular level. gamma-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 gamma-tubulin are associated in the gamma-tubulin complexes. (3) gamma-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 gamma-tubulin appears associated with at least three evolutionary related centrosomal proteins, raising new questions about their functions at the molecular level.
pubmed:commentsCorrections
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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
147
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
857-68
pubmed:dateRevised
2011-6-20
pubmed:meshHeading
pubmed-meshheading:10562286-Amino Acid Sequence, pubmed-meshheading:10562286-Animals, pubmed-meshheading:10562286-Brain, pubmed-meshheading:10562286-COS Cells, pubmed-meshheading:10562286-Centrosome, pubmed-meshheading:10562286-DNA, Complementary, pubmed-meshheading:10562286-Drosophila, pubmed-meshheading:10562286-Humans, pubmed-meshheading:10562286-Medicago sativa, pubmed-meshheading:10562286-Microtubule-Associated Proteins, pubmed-meshheading:10562286-Microtubules, pubmed-meshheading:10562286-Molecular Sequence Data, pubmed-meshheading:10562286-Open Reading Frames, pubmed-meshheading:10562286-Recombinant Fusion Proteins, pubmed-meshheading:10562286-Sequence Alignment, pubmed-meshheading:10562286-Sequence Homology, Amino Acid, pubmed-meshheading:10562286-Sheep, pubmed-meshheading:10562286-Swine, pubmed-meshheading:10562286-Transfection, pubmed-meshheading:10562286-Tubulin
pubmed:year
1999
pubmed:articleTitle
Human 76p: A new member of the gamma-tubulin-associated protein family.
pubmed:affiliation
Institut de Pharmacologie et de Biologie Structurale, Centre National de la Recherche Scientifique, 31400 Toulouse, France.
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