Optical Control of G-Actin with a Photoswitchable Latrunculin.
Journal
bioRxiv : the preprint server for biology
Titre abrégé: bioRxiv
Pays: United States
ID NLM: 101680187
Informations de publication
Date de publication:
19 Jul 2023
19 Jul 2023
Historique:
pubmed:
28
7
2023
medline:
28
7
2023
entrez:
28
7
2023
Statut:
epublish
Résumé
Actin is one of the most abundant proteins in eukaryotic cells and a key component of the cytoskeleton. A range of small molecules have emerged that interfere with actin dynamics by either binding to polymeric F-actin or monomeric G-actin to stabilize or destabilize filaments or prevent their formation and growth, respectively. Amongst these, the latrunculins, which bind to G-actin and affect polymerization, are widely used as tools to investigate actin-dependent cellular processes. Here, we report a photoswitchable version of latrunculin, termed opto-latrunculin (
Identifiants
pubmed: 37502978
doi: 10.1101/2023.07.17.549222
pmc: PMC10370057
pii:
doi:
Types de publication
Preprint
Langues
eng
Subventions
Organisme : NIGMS NIH HHS
ID : T32 GM007365
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM126228
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS119823
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM122589
Pays : United States
Organisme : NIA NIH HHS
ID : R21 AG051047
Pays : United States
Organisme : NIA NIH HHS
ID : R33 AG051047
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA013696
Pays : United States