Characterization of unique functionalities in c-Src domains required for osteoclast podosome belt formation.
Src
Src homology 2 domain (SH2 domain)
Src homology 3 domain (SH3 domain)
osteoclast
podosome
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
Historique:
received:
01
09
2020
revised:
03
05
2021
accepted:
12
05
2021
pubmed:
22
5
2021
medline:
1
9
2021
entrez:
21
5
2021
Statut:
ppublish
Résumé
Deletion of c-Src, a ubiquitously expressed tyrosine kinase, results in osteoclast dysfunction and osteopetrosis, in which bones harden into "stone." In contrast, deletion of the genes encoding other members of the Src family kinase (SFK) fails to produce an osteopetrotic phenotype. This suggests that c-Src performs a unique function in the osteoclast that cannot be compensated for by other SFKs. We aimed to identify the molecular basis of this unique role in osteoclasts and bone resorption. We found that c-Src, Lyn, and Fyn were the most highly expressed SFKs in WT osteoclasts, whereas Hck, Lck, Blk, and Fgr displayed low levels of expression. Formation of the podosome belt, clusters of unique actin assemblies, was disrupted in src
Identifiants
pubmed: 34019873
pii: S0021-9258(21)00583-4
doi: 10.1016/j.jbc.2021.100790
pmc: PMC8196221
pii:
doi:
Substances chimiques
src-Family Kinases
EC 2.7.10.2
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
100790Subventions
Organisme : NIAMS NIH HHS
ID : R01 AR042927
Pays : United States
Organisme : NIAMS NIH HHS
ID : R01 AR062054
Pays : United States
Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
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