Microtubule Plus End Dynamics - Do We Know How Microtubules Grow?: Cells boost microtubule growth by promoting distinct structural transitions at growing microtubule ends.
Animals
Cell Line, Tumor
Cryoelectron Microscopy
Doublecortin Domain Proteins
Guanosine
/ chemistry
Guanosine Triphosphate
/ chemistry
Humans
Hydrolysis
Mammals
Microtubule-Associated Proteins
/ metabolism
Microtubules
/ metabolism
Models, Molecular
Morphogenesis
Neuropeptides
/ metabolism
Polymerization
Protein Binding
Protein Conformation
Tubulin
/ chemistry
Tubulin Modulators
/ metabolism
CKAP5
cytoskeleton
doublecortin
end-binding proteins
microtubule
microtubule dynamics
Journal
BioEssays : news and reviews in molecular, cellular and developmental biology
ISSN: 1521-1878
Titre abrégé: Bioessays
Pays: United States
ID NLM: 8510851
Informations de publication
Date de publication:
03 2019
03 2019
Historique:
received:
24
09
2018
revised:
22
12
2018
pubmed:
8
2
2019
medline:
18
12
2019
entrez:
8
2
2019
Statut:
ppublish
Résumé
Microtubules form a highly dynamic filament network in all eukaryotic cells. Individual microtubules grow by tubulin dimer subunit addition and frequently switch between phases of growth and shortening. These unique dynamics are powered by GTP hydrolysis and drive microtubule network remodeling, which is central to eukaryotic cell biology and morphogenesis. Yet, our knowledge of the molecular events at growing microtubule ends remains incomplete. Here, recent ultrastructural, biochemical and cell biological data are integrated to develop a realistic model of growing microtubule ends comprised of structurally distinct but biochemically overlapping zones. Proteins that recognize microtubule lattice conformations associated with specific tubulin guanosine nucleotide states may independently control major structural transitions at growing microtubule ends. A model is proposed in which tubulin dimer addition and subsequent closure of the MT wall are optimized in cells to achieve rapid physiological microtubule growth.
Identifiants
pubmed: 30730055
doi: 10.1002/bies.201800194
pmc: PMC7021488
mid: NIHMS1067364
doi:
Substances chimiques
CKAP5 protein, human
0
Doublecortin Domain Proteins
0
Microtubule-Associated Proteins
0
Neuropeptides
0
Tubulin
0
Tubulin Modulators
0
Guanosine
12133JR80S
Guanosine Triphosphate
86-01-1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
e1800194Subventions
Organisme : NINDS NIH HHS
ID : R01 NS107480
Pays : United States
Organisme : NCRR NIH HHS
ID : S10 RR026758
Pays : United States
Informations de copyright
© 2019 WILEY Periodicals, Inc.
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